메뉴 건너뛰기




Volumn 1, Issue , 2012, Pages 277-310

Analysis of 2-D crystals of membrane proteins by electron microscopy

Author keywords

2 D crystallization; 3 D structure determination; Electron crystallography; Electron microscopy; Expression; Image processing; Membrane proteins; Purification

Indexed keywords


EID: 84882792762     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374920-8.00119-3     Document Type: Chapter
Times cited : (11)

References (319)
  • 1
    • 0028175266 scopus 로고
    • Biologically active two-dimensional crystals of aquaporin CHIP
    • Walz T., Smith B., Zeidel M., Engel A., Agre P. Biologically active two-dimensional crystals of aquaporin CHIP. J. Biol. Chem. 1994, 269(3):1583-1586.
    • (1994) J. Biol. Chem. , vol.269 , Issue.3 , pp. 1583-1586
    • Walz, T.1    Smith, B.2    Zeidel, M.3    Engel, A.4    Agre, P.5
  • 2
    • 0026506038 scopus 로고
    • Two-dimensional crystallization of membrane proteins
    • Kühlbrandt W. Two-dimensional crystallization of membrane proteins. Quart. Rev. Biophys. 1992, 25(1):1-49.
    • (1992) Quart. Rev. Biophys. , vol.25 , Issue.1 , pp. 1-49
    • Kühlbrandt, W.1
  • 5
    • 66249098524 scopus 로고    scopus 로고
    • Membrane protein biophysics
    • Anson L. Membrane protein biophysics. Nature 2009, 459(7245):343.
    • (2009) Nature , vol.459 , Issue.7245 , pp. 343
    • Anson, L.1
  • 6
    • 0026049814 scopus 로고
    • Proper and improper folding of proteins in the cellular environment
    • Nilsson B., Anderson S. Proper and improper folding of proteins in the cellular environment. Annu. Rev. Microbiol. 1991, 45:607-635.
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 607-635
    • Nilsson, B.1    Anderson, S.2
  • 7
    • 0023189083 scopus 로고
    • Multicopy expression vectors carrying the lac repressor gene for regulated high-level expression of genes in Escherichia coli
    • Stark M.J. Multicopy expression vectors carrying the lac repressor gene for regulated high-level expression of genes in Escherichia coli. Gene 1987, 51(2-3):255-267.
    • (1987) Gene , vol.51 , Issue.2-3 , pp. 255-267
    • Stark, M.J.1
  • 8
    • 65449158090 scopus 로고    scopus 로고
    • Biochemical and structural analysis of bacterial O-antigen chain length regulator proteins reveals a conserved quaternary structure
    • Larue K., Kimber M.S., Ford R., Whitfield C. Biochemical and structural analysis of bacterial O-antigen chain length regulator proteins reveals a conserved quaternary structure. J. Biol. Chem. 2009, 284(11):7395-7403.
    • (2009) J. Biol. Chem. , vol.284 , Issue.11 , pp. 7395-7403
    • Larue, K.1    Kimber, M.S.2    Ford, R.3    Whitfield, C.4
  • 10
    • 34347393962 scopus 로고    scopus 로고
    • Conditions that allow for effective transfer of membrane proteins onto nitrocellulose membrane in Western blots
    • Abeyrathne P.D., Lam J.S. Conditions that allow for effective transfer of membrane proteins onto nitrocellulose membrane in Western blots. Can. J. Microbiol. 2007, 53(4):526-532.
    • (2007) Can. J. Microbiol. , vol.53 , Issue.4 , pp. 526-532
    • Abeyrathne, P.D.1    Lam, J.S.2
  • 11
    • 34848814808 scopus 로고    scopus 로고
    • Biochemical characterization of MsbA from Pseudomonas aeruginosa
    • Ghanei H., Abeyrathne P.D., Lam J.S. Biochemical characterization of MsbA from Pseudomonas aeruginosa. J. Biol. Chem. 2007, 282(37):26939-26947.
    • (2007) J. Biol. Chem. , vol.282 , Issue.37 , pp. 26939-26947
    • Ghanei, H.1    Abeyrathne, P.D.2    Lam, J.S.3
  • 12
    • 62049085752 scopus 로고    scopus 로고
    • Oligomeric structure and functional characterization of the urea transporter from Actinobacillus pleuropneumoniae
    • Raunser S., Mathai J.C., Abeyrathne P.D., Rice A.J., Zeidel M.L., Walz T. Oligomeric structure and functional characterization of the urea transporter from Actinobacillus pleuropneumoniae. J. Mol. Biol. 2009, 387(3):619-627.
    • (2009) J. Mol. Biol. , vol.387 , Issue.3 , pp. 619-627
    • Raunser, S.1    Mathai, J.C.2    Abeyrathne, P.D.3    Rice, A.J.4    Zeidel, M.L.5    Walz, T.6
  • 14
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B., Walker J.E. Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 1996, 260(3):289-298.
    • (1996) J. Mol. Biol. , vol.260 , Issue.3 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 15
    • 0037450548 scopus 로고    scopus 로고
    • The expression of outer membrane proteins for crystallization
    • Bannwarth M., Schulz G.E. The expression of outer membrane proteins for crystallization. Biochim. Biophys. Acta 2003, 1610(1):37-45.
    • (2003) Biochim. Biophys. Acta , vol.1610 , Issue.1 , pp. 37-45
    • Bannwarth, M.1    Schulz, G.E.2
  • 16
    • 0037391134 scopus 로고    scopus 로고
    • Membrane protein structural biology: The high throughput challenge
    • Loll P.J. Membrane protein structural biology: The high throughput challenge. J. Struct. Biol. 2003, 142(1):144-153.
    • (2003) J. Struct. Biol. , vol.142 , Issue.1 , pp. 144-153
    • Loll, P.J.1
  • 17
    • 0027361998 scopus 로고
    • Expression of a rat neurotensin receptor in Escherichia coli
    • Grisshammer R., Duckworth R., Henderson R. Expression of a rat neurotensin receptor in Escherichia coli. Biochem. J. 1993, 295(Pt 2):571-576.
    • (1993) Biochem. J. , vol.295 , Issue.PT 2 , pp. 571-576
    • Grisshammer, R.1    Duckworth, R.2    Henderson, R.3
  • 18
    • 0029838532 scopus 로고    scopus 로고
    • Purification of a rat neurotensin receptor expressed in Escherichia coli
    • Tucker J., Grisshammer R. Purification of a rat neurotensin receptor expressed in Escherichia coli. Biochem. J. 1996, 317(Pt 3):891-899.
    • (1996) Biochem. J. , vol.317 , Issue.PT 3 , pp. 891-899
    • Tucker, J.1    Grisshammer, R.2
  • 19
    • 12244292640 scopus 로고    scopus 로고
    • Purification and characterization of the human adenosine A(2a) receptor functionally expressed in Escherichia coli
    • Weiss H.M., Grisshammer R. Purification and characterization of the human adenosine A(2a) receptor functionally expressed in Escherichia coli. Eur. J. Biochem 2002, 269(1):82-92.
    • (2002) Eur. J. Biochem , vol.269 , Issue.1 , pp. 82-92
    • Weiss, H.M.1    Grisshammer, R.2
  • 20
    • 0030467888 scopus 로고    scopus 로고
    • Expression of an olfactory receptor in Escherichia coli: Purification, reconstitution, and ligand binding
    • Kiefer H., Krieger J., Olszewski J.D., Von Heijne G., Prestwich G.D., Breer H. Expression of an olfactory receptor in Escherichia coli: Purification, reconstitution, and ligand binding. Biochemistry 1996, 35(50):16077-16084.
    • (1996) Biochemistry , vol.35 , Issue.50 , pp. 16077-16084
    • Kiefer, H.1    Krieger, J.2    Olszewski, J.D.3    Von Heijne, G.4    Prestwich, G.D.5    Breer, H.6
  • 21
    • 0030707872 scopus 로고    scopus 로고
    • The human RAE1 gene is a functional homologue of Schizosaccharomyces pombe rae1 gene involved in nuclear export of Poly(A)+ RNA
    • Bharathi A., Ghosh A., Whalen W.A., Yoon J.H., Pu R., Dasso M., Dhar R. The human RAE1 gene is a functional homologue of Schizosaccharomyces pombe rae1 gene involved in nuclear export of Poly(A)+ RNA. Gene 1997, 198(1-2):251-258.
    • (1997) Gene , vol.198 , Issue.1-2 , pp. 251-258
    • Bharathi, A.1    Ghosh, A.2    Whalen, W.A.3    Yoon, J.H.4    Pu, R.5    Dasso, M.6    Dhar, R.7
  • 23
    • 2442625216 scopus 로고    scopus 로고
    • Choosing and using Schizosaccharomyces pombe plasmids
    • Siam R., Dolan W.P., Forsburg S.L. Choosing and using Schizosaccharomyces pombe plasmids. Methods 2004, 33(3):189-198.
    • (2004) Methods , vol.33 , Issue.3 , pp. 189-198
    • Siam, R.1    Dolan, W.P.2    Forsburg, S.L.3
  • 24
    • 0031172606 scopus 로고    scopus 로고
    • Functional expression of bovine opsin in the methylotrophic yeast Pichia pastoris
    • Abdulaev N.G., Popp M.P., Smith W.C., Ridge K.D. Functional expression of bovine opsin in the methylotrophic yeast Pichia pastoris. Protein Expr. Purif. 1997, 10(1):61-69.
    • (1997) Protein Expr. Purif. , vol.10 , Issue.1 , pp. 61-69
    • Abdulaev, N.G.1    Popp, M.P.2    Smith, W.C.3    Ridge, K.D.4
  • 25
    • 0028847201 scopus 로고
    • Co-expression of the neurokinin NK2 receptor and G-protein components in the fission yeast Schizosaccharomyces pombe
    • Arkinstall S., Edgerton M., Payton M., Maundrell K. Co-expression of the neurokinin NK2 receptor and G-protein components in the fission yeast Schizosaccharomyces pombe. FEBS Lett. 1995, 375(3):183-187.
    • (1995) FEBS Lett. , vol.375 , Issue.3 , pp. 183-187
    • Arkinstall, S.1    Edgerton, M.2    Payton, M.3    Maundrell, K.4
  • 26
    • 0034998457 scopus 로고    scopus 로고
    • Functional expression of M(1), M(3) and M(5) muscarinic acetylcholine receptors in yeast
    • Erlenbach I., Kostenis E., Schmidt C., Hamdan F.F., Pausch M.H., Wess J. Functional expression of M(1), M(3) and M(5) muscarinic acetylcholine receptors in yeast. J. Neurochem. 2001, 77(5):1327-1337.
    • (2001) J. Neurochem. , vol.77 , Issue.5 , pp. 1327-1337
    • Erlenbach, I.1    Kostenis, E.2    Schmidt, C.3    Hamdan, F.F.4    Pausch, M.H.5    Wess, J.6
  • 27
    • 0029859488 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Expression of functional mammalian opsin in Saccharomyces cerevisiae
    • Mollaaghababa R., Davidson F.F., Kaiser C., Khorana H.G. Structure and function in rhodopsin: Expression of functional mammalian opsin in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 1996, 93(21):11482-11486.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , Issue.21 , pp. 11482-11486
    • Mollaaghababa, R.1    Davidson, F.F.2    Kaiser, C.3    Khorana, H.G.4
  • 28
    • 0025315790 scopus 로고
    • Expression and pharmacological characterization of the human M1 muscarinic receptor in Saccharomyces cerevisiae
    • Payette P., Gossard F., Whiteway M., Dennis M. Expression and pharmacological characterization of the human M1 muscarinic receptor in Saccharomyces cerevisiae. FEBS Lett. 1990, 266(1-2):21-25.
    • (1990) FEBS Lett. , vol.266 , Issue.1-2 , pp. 21-25
    • Payette, P.1    Gossard, F.2    Whiteway, M.3    Dennis, M.4
  • 29
    • 0032148392 scopus 로고    scopus 로고
    • Pharmacological characterisation of the D2 dopamine receptor expressed in the yeast Schizosaccharomyces pombe
    • Presland J., Strange P.G. Pharmacological characterisation of the D2 dopamine receptor expressed in the yeast Schizosaccharomyces pombe. Biochem. Pharmacol. 1998, 56(5):577-582.
    • (1998) Biochem. Pharmacol. , vol.56 , Issue.5 , pp. 577-582
    • Presland, J.1    Strange, P.G.2
  • 30
    • 0028070288 scopus 로고
    • Constitutive expression of the human D2S-dopamine receptor in the unicellular yeast Saccharomyces cerevisiae
    • Sander P., Grunewald S., Maul G., Reilander H., Michel H. Constitutive expression of the human D2S-dopamine receptor in the unicellular yeast Saccharomyces cerevisiae. Biochim. Biophys. Acta 1994, 1193(2):255-262.
    • (1994) Biochim. Biophys. Acta , vol.1193 , Issue.2 , pp. 255-262
    • Sander, P.1    Grunewald, S.2    Maul, G.3    Reilander, H.4    Michel, H.5
  • 32
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • Cereghino J.L., Cregg J.M. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 2000, 24(1):45-66.
    • (2000) FEMS Microbiol. Rev. , vol.24 , Issue.1 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 33
    • 0141457531 scopus 로고    scopus 로고
    • + channels heterologously expressed in Pichia pastoris
    • + channels heterologously expressed in Pichia pastoris. J. Mol. Biol. 2003, 333(1):103-116.
    • (2003) J. Mol. Biol. , vol.333 , Issue.1 , pp. 103-116
    • Parcej, D.N.1    Eckhardt-Strelau, L.2
  • 34
    • 0042693016 scopus 로고    scopus 로고
    • Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures
    • Binda C., Li M., Hubalek F., Restelli N., Edmondson D.E., Mattevi A. Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures. Proc. Natl. Acad. Sci. USA 2003, 100(17):9750-9755.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.17 , pp. 9750-9755
    • Binda, C.1    Li, M.2    Hubalek, F.3    Restelli, N.4    Edmondson, D.E.5    Mattevi, A.6
  • 36
    • 55749110716 scopus 로고    scopus 로고
    • Production of membrane proteins using cell-free expression systems
    • Schwarz D., Dotsch V., Bernhard F. Production of membrane proteins using cell-free expression systems. Proteomics 2008, 8(19):3933-3946.
    • (2008) Proteomics , vol.8 , Issue.19 , pp. 3933-3946
    • Schwarz, D.1    Dotsch, V.2    Bernhard, F.3
  • 37
    • 4744351698 scopus 로고    scopus 로고
    • Cell-free synthesis of a functional ion channel in the absence of a membrane and in the presence of detergent
    • Berrier C., Park K.H., Abes S., Bibonne A., Betton J.M., Ghazi A. Cell-free synthesis of a functional ion channel in the absence of a membrane and in the presence of detergent. Biochemistry 2004, 43(39):12585-12591.
    • (2004) Biochemistry , vol.43 , Issue.39 , pp. 12585-12591
    • Berrier, C.1    Park, K.H.2    Abes, S.3    Bibonne, A.4    Betton, J.M.5    Ghazi, A.6
  • 38
    • 1242319564 scopus 로고    scopus 로고
    • In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state
    • Elbaz Y., Steiner-Mordoch S., Danieli T., Schuldiner S. In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state. Proc. Natl. Acad. Sci. USA 2004, 101(6):1519-1524.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , Issue.6 , pp. 1519-1524
    • Elbaz, Y.1    Steiner-Mordoch, S.2    Danieli, T.3    Schuldiner, S.4
  • 39
    • 15744391469 scopus 로고    scopus 로고
    • Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors
    • Ishihara G., Goto M., Saeki M., Ito K., Hori T., Kigawa T., Shirouzu M., Yokoyama S. Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors. Protein Expr. Purif. 2005, 41(1):27-37.
    • (2005) Protein Expr. Purif. , vol.41 , Issue.1 , pp. 27-37
    • Ishihara, G.1    Goto, M.2    Saeki, M.3    Ito, K.4    Hori, T.5    Kigawa, T.6    Shirouzu, M.7    Yokoyama, S.8
  • 42
    • 28244458078 scopus 로고    scopus 로고
    • Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system
    • Klammt C., Schwarz D., Fendler K., Haase W., Dotsch V., Bernhard F. Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system. FEBS. J. 2005, 272(23):6024-6038.
    • (2005) FEBS. J. , vol.272 , Issue.23 , pp. 6024-6038
    • Klammt, C.1    Schwarz, D.2    Fendler, K.3    Haase, W.4    Dotsch, V.5    Bernhard, F.6
  • 43
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • Spirin A.S., Baranov V.I., Ryabova L.A., Ovodov S.Y., Alakhov Y.B. A continuous cell-free translation system capable of producing polypeptides in high yield. Science 1988, 242(4882):1162-1164.
    • (1988) Science , vol.242 , Issue.4882 , pp. 1162-1164
    • Spirin, A.S.1    Baranov, V.I.2    Ryabova, L.A.3    Ovodov, S.Y.4    Alakhov, Y.B.5
  • 44
    • 25844528201 scopus 로고    scopus 로고
    • Efficient strategy for the rapid backbone assignment of membrane proteins
    • Trbovic N., Klammt C., Koglin A., Lohr F., Bernhard F., Dotsch V. Efficient strategy for the rapid backbone assignment of membrane proteins. J. Am. Chem. Soc. 2005, 127(39):13504-13505.
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.39 , pp. 13504-13505
    • Trbovic, N.1    Klammt, C.2    Koglin, A.3    Lohr, F.4    Bernhard, F.5    Dotsch, V.6
  • 45
    • 33746256604 scopus 로고    scopus 로고
    • Combination of cell-free expression and NMR spectroscopy as a new approach for structural investigation of membrane proteins
    • Spec No, S17-S23
    • Koglin A., Klammt C., Trbovic N., Schwarz D., Schneider B., Schafer B., Lohr F., Bernhard F., Dotsch V. Combination of cell-free expression and NMR spectroscopy as a new approach for structural investigation of membrane proteins. Magn. Reson. Chem. 2006, 44. Spec No, S17-S23.
    • (2006) Magn. Reson. Chem. , vol.44
    • Koglin, A.1    Klammt, C.2    Trbovic, N.3    Schwarz, D.4    Schneider, B.5    Schafer, B.6    Lohr, F.7    Bernhard, F.8    Dotsch, V.9
  • 46
    • 33751293464 scopus 로고    scopus 로고
    • Solubilization and Purification of Membrane Proteins
    • CRC Press, Boca Raton, K. Lundstrom (Ed.)
    • Byrne B., Jormakka M. Solubilization and Purification of Membrane Proteins. Structural Genomics on Membrane Proteins 2006, 179-198. CRC Press, Boca Raton. K. Lundstrom (Ed.).
    • (2006) Structural Genomics on Membrane Proteins , pp. 179-198
    • Byrne, B.1    Jormakka, M.2
  • 49
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues
    • Hochuli E., Dobeli H., Schacher A. New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues. J. Chromatogr. 1987, 411:177-184.
    • (1987) J. Chromatogr. , vol.411 , pp. 177-184
    • Hochuli, E.1    Dobeli, H.2    Schacher, A.3
  • 50
    • 0021259905 scopus 로고
    • Cobalt-ion chelate affinity chromatography for the purification of brain neutral alpha-D-mannosidase and its separation from acid alpha-D-mannosidase
    • Mathur R., Balasubramanian A.S. Cobalt-ion chelate affinity chromatography for the purification of brain neutral alpha-D-mannosidase and its separation from acid alpha-D-mannosidase. Biochem. J. 1984, 222(1):261-264.
    • (1984) Biochem. J. , vol.222 , Issue.1 , pp. 261-264
    • Mathur, R.1    Balasubramanian, A.S.2
  • 51
    • 0028241136 scopus 로고
    • Purification of two active fusion proteins of the Na(+)-dependent citrate carrier of Klebsiella pneumoniae
    • Pos K.M., Bott M., Dimroth P. Purification of two active fusion proteins of the Na(+)-dependent citrate carrier of Klebsiella pneumoniae. FEBS Lett. 1994, 347(1):37-41.
    • (1994) FEBS Lett. , vol.347 , Issue.1 , pp. 37-41
    • Pos, K.M.1    Bott, M.2    Dimroth, P.3
  • 53
    • 33847063568 scopus 로고    scopus 로고
    • Projection map of aquaporin-9 at 7 A resolution
    • Viadiu H., Gonen T., Walz T. Projection map of aquaporin-9 at 7 A resolution. J. Mol. Biol. 2007, 367(1):80-88.
    • (2007) J. Mol. Biol. , vol.367 , Issue.1 , pp. 80-88
    • Viadiu, H.1    Gonen, T.2    Walz, T.3
  • 56
    • 0343550381 scopus 로고    scopus 로고
    • Purification and two-dimensional crystallization of highly active cytochrome b(6)f complex from spinach
    • Dietrich J., Kuhlbrandt W. Purification and two-dimensional crystallization of highly active cytochrome b(6)f complex from spinach. FEBS Lett 1999, 463(1-2):97-102.
    • (1999) FEBS Lett , vol.463 , Issue.1-2 , pp. 97-102
    • Dietrich, J.1    Kuhlbrandt, W.2
  • 58
    • 0033168715 scopus 로고    scopus 로고
    • Projection structure of NhaA, a secondary transporter from Escherichia coli, at 4.0 A resolution
    • Williams K.A., Geldmacher-Kaufer U., Padan E., Schuldiner S., Kühlbrandt W. Projection structure of NhaA, a secondary transporter from Escherichia coli, at 4.0 A resolution. EMBO J. 1999, 18(13):3558-3563.
    • (1999) EMBO J. , vol.18 , Issue.13 , pp. 3558-3563
    • Williams, K.A.1    Geldmacher-Kaufer, U.2    Padan, E.3    Schuldiner, S.4    Kühlbrandt, W.5
  • 59
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • Nogales E., Wolf S.G., Downing K.H. Structure of the alpha beta tubulin dimer by electron crystallography. Nature 1998, 391(6663):199-203.
    • (1998) Nature , vol.391 , Issue.6663 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 60
    • 0029063397 scopus 로고
    • Structure of tubulin at 6.5 A and location of the taxol-binding site
    • Nogales E., Wolf S.G., Khan I.A., Luduena R.F., Downing K.H. Structure of tubulin at 6.5 A and location of the taxol-binding site. Nature 1995, 375(6530):424-427.
    • (1995) Nature , vol.375 , Issue.6530 , pp. 424-427
    • Nogales, E.1    Wolf, S.G.2    Khan, I.A.3    Luduena, R.F.4    Downing, K.H.5
  • 61
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4A resolution
    • Unwin N. Refined structure of the nicotinic acetylcholine receptor at 4A resolution. J. Mol. Biol. 2005, 346(4):967-989.
    • (2005) J. Mol. Biol. , vol.346 , Issue.4 , pp. 967-989
    • Unwin, N.1
  • 63
    • 0034610788 scopus 로고    scopus 로고
    • Three-dimensional structure of the ion-coupled transport protein NhaA
    • Williams K.A. Three-dimensional structure of the ion-coupled transport protein NhaA. Nature 2000, 403(6765):112-115.
    • (2000) Nature , vol.403 , Issue.6765 , pp. 112-115
    • Williams, K.A.1
  • 65
    • 0035239217 scopus 로고    scopus 로고
    • Structure and mass analysis by scanning transmission electron microscopy
    • Müller S.A., Engel A. Structure and mass analysis by scanning transmission electron microscopy. Micron 2001, 32(1):21-31.
    • (2001) Micron , vol.32 , Issue.1 , pp. 21-31
    • Müller, S.A.1    Engel, A.2
  • 66
    • 0020754427 scopus 로고
    • The structure of membrane crystals of the light-harvesting chlorophyll a/b protein complex
    • Kühlbrandt W., Thaler T., Wehrli E. The structure of membrane crystals of the light-harvesting chlorophyll a/b protein complex. J. Cell Biol. 1983, 96(5):1414-1424.
    • (1983) J. Cell Biol. , vol.96 , Issue.5 , pp. 1414-1424
    • Kühlbrandt, W.1    Thaler, T.2    Wehrli, E.3
  • 67
    • 0034608009 scopus 로고    scopus 로고
    • Conformational changes in the cytochrome b6f complex induced by inhibitor binding
    • Breyton C. Conformational changes in the cytochrome b6f complex induced by inhibitor binding. J. Biol. Chem. 2000, 275(18):13195-13201.
    • (2000) J. Biol. Chem. , vol.275 , Issue.18 , pp. 13195-13201
    • Breyton, C.1
  • 68
    • 0033582824 scopus 로고    scopus 로고
    • The 9 A projection structure of cytochrome b6f complex determined by electron crystallography
    • Bron P., Lacapere J.J., Breyton C., Mosser G. The 9 A projection structure of cytochrome b6f complex determined by electron crystallography. J. Mol. Biol. 1999, 287(1):117-126.
    • (1999) J. Mol. Biol. , vol.287 , Issue.1 , pp. 117-126
    • Bron, P.1    Lacapere, J.J.2    Breyton, C.3    Mosser, G.4
  • 69
    • 0030753749 scopus 로고    scopus 로고
    • Projection map of cytochrome b6 f complex at 8 A resolution
    • Mosser G., Breyton C., Olofsson A., Popot J.L., Rigaud J.L. Projection map of cytochrome b6 f complex at 8 A resolution. J. Biol. Chem. 1997, 272(32):20263-20268.
    • (1997) J. Biol. Chem. , vol.272 , Issue.32 , pp. 20263-20268
    • Mosser, G.1    Breyton, C.2    Olofsson, A.3    Popot, J.L.4    Rigaud, J.L.5
  • 70
    • 0019878401 scopus 로고
    • Membrane crystals of a subunit complex of mitochondrial cytochrome reductase containing the cytochromes b and c1
    • Hovmöller S., Leonard K., Weiss H. Membrane crystals of a subunit complex of mitochondrial cytochrome reductase containing the cytochromes b and c1. FEBS Lett. 1981, 123(1):118-122.
    • (1981) FEBS Lett. , vol.123 , Issue.1 , pp. 118-122
    • Hovmöller, S.1    Leonard, K.2    Weiss, H.3
  • 71
    • 0039952981 scopus 로고    scopus 로고
    • Two-dimensional crystallization of Ca-ATPase by detergent removal
    • Lacapere J.J., Stokes D.L., Olofsson A., Rigaud J.L. Two-dimensional crystallization of Ca-ATPase by detergent removal. Biophys. J. 1998, 75(3):1319-1329.
    • (1998) Biophys. J. , vol.75 , Issue.3 , pp. 1319-1329
    • Lacapere, J.J.1    Stokes, D.L.2    Olofsson, A.3    Rigaud, J.L.4
  • 74
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
    • Essen L., Siegert R., Lehmann W.D., Oesterhelt D. Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex. Proc. Natl. Acad. Sci. USA 1998, 95(20):11673-11678.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.20 , pp. 11673-11678
    • Essen, L.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 75
    • 0034660152 scopus 로고    scopus 로고
    • Structure at 2.3 Å resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment
    • Hunte C., Koepke J., Lange C., Rossmanith T., Michel H. Structure at 2.3 Å resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment. Struct. Fold. Des 2000, 8(6):669-684.
    • (2000) Struct. Fold. Des , vol.8 , Issue.6 , pp. 669-684
    • Hunte, C.1    Koepke, J.2    Lange, C.3    Rossmanith, T.4    Michel, H.5
  • 76
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
    • Jordan P., Fromme P., Witt H.T., Klukas O., Saenger W., Krau B.N. Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 2001, 411(6840):909-917.
    • (2001) Nature , vol.411 , Issue.6840 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krau, B.N.6
  • 77
    • 28444450878 scopus 로고    scopus 로고
    • Lipid-protein interactions in double-layered two-dimensional AQP0 crystals
    • Gonen T., Cheng Y., Sliz P., Hiroaki Y., Fujiyoshi Y., Harrison S.C., Walz T. Lipid-protein interactions in double-layered two-dimensional AQP0 crystals. Nature 2005, 438(7068):633-638.
    • (2005) Nature , vol.438 , Issue.7068 , pp. 633-638
    • Gonen, T.1    Cheng, Y.2    Sliz, P.3    Hiroaki, Y.4    Fujiyoshi, Y.5    Harrison, S.C.6    Walz, T.7
  • 78
    • 77952584138 scopus 로고    scopus 로고
    • Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2-D crystals
    • Hite R.K., Li Z., Walz T. Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2-D crystals. EMBO J. 2010, 29(10):1652-1658.
    • (2010) EMBO J. , vol.29 , Issue.10 , pp. 1652-1658
    • Hite, R.K.1    Li, Z.2    Walz, T.3
  • 79
    • 0027452052 scopus 로고
    • Lipid-protein interactions in crystals of plant light-harvesting complex
    • Nussberger S., Dorr K., Wang D.N., Kühlbrandt W. Lipid-protein interactions in crystals of plant light-harvesting complex. J. Mol. Biol. 1993, 234(2):347-356.
    • (1993) J. Mol. Biol. , vol.234 , Issue.2 , pp. 347-356
    • Nussberger, S.1    Dorr, K.2    Wang, D.N.3    Kühlbrandt, W.4
  • 80
    • 0029923428 scopus 로고    scopus 로고
    • Two-dimensional crystallization and cryo-electron microscopy of photosystem II
    • Nakazato K., Toyoshima C., Enami I., Inoue Y. Two-dimensional crystallization and cryo-electron microscopy of photosystem II. J. Mol. Biol. 1996, 257(2):225-232.
    • (1996) J. Mol. Biol. , vol.257 , Issue.2 , pp. 225-232
    • Nakazato, K.1    Toyoshima, C.2    Enami, I.3    Inoue, Y.4
  • 81
    • 0032548142 scopus 로고    scopus 로고
    • Three-dimensional structure of the plant photosystem II reaction centre at 8 A resolution
    • Rhee K.H., Morris E.P., Barber J., Kühlbrandt W. Three-dimensional structure of the plant photosystem II reaction centre at 8 A resolution. Nature 1998, 396(6708):283-286.
    • (1998) Nature , vol.396 , Issue.6708 , pp. 283-286
    • Rhee, K.H.1    Morris, E.P.2    Barber, J.3    Kühlbrandt, W.4
  • 83
    • 38849171893 scopus 로고    scopus 로고
    • NMR spectroscopic and analytical ultracentrifuge analysis of membrane protein detergent complexes
    • Maslennikov I., Kefala G., Johnson C., Riek R., Choe S., Kwiatkowski W. NMR spectroscopic and analytical ultracentrifuge analysis of membrane protein detergent complexes. BMC Struct. Biol. 2007, 7:74.
    • (2007) BMC Struct. Biol. , vol.7 , pp. 74
    • Maslennikov, I.1    Kefala, G.2    Johnson, C.3    Riek, R.4    Choe, S.5    Kwiatkowski, W.6
  • 85
    • 0000768433 scopus 로고    scopus 로고
    • Two-dimensional crystallization of membrane proteins
    • Oxford University Press, Oxford, GBR, S.A. Baldwin (Ed.)
    • Ringler P., Heymann B.J., Engel A. Two-dimensional crystallization of membrane proteins. Membrane Transport 2000, 229-268. Oxford University Press, Oxford, GBR. S.A. Baldwin (Ed.).
    • (2000) Membrane Transport , pp. 229-268
    • Ringler, P.1    Heymann, B.J.2    Engel, A.3
  • 86
    • 0035141545 scopus 로고    scopus 로고
    • Two-dimensional crystallogenesis of transmembrane proteins
    • Mosser G. Two-dimensional crystallogenesis of transmembrane proteins. Micron 2001, 32(5):517-540.
    • (2001) Micron , vol.32 , Issue.5 , pp. 517-540
    • Mosser, G.1
  • 87
    • 0344983317 scopus 로고    scopus 로고
    • Projection structure of the bacterial oxalate transporter OxlT at 3.4A resolution
    • Heymann J.A., Hirai T., Shi D., Subramaniam S. Projection structure of the bacterial oxalate transporter OxlT at 3.4A resolution. J. Struct. Biol. 2003, 144(3):320-326.
    • (2003) J. Struct. Biol. , vol.144 , Issue.3 , pp. 320-326
    • Heymann, J.A.1    Hirai, T.2    Shi, D.3    Subramaniam, S.4
  • 90
    • 0025297219 scopus 로고
    • Structure of PhoE porin in projection at 3.5 A resolution
    • Jap B.K., Downing K.H., Walian P.J. Structure of PhoE porin in projection at 3.5 A resolution. J. Struct. Biol. 1990, 103(1):57-63.
    • (1990) J. Struct. Biol. , vol.103 , Issue.1 , pp. 57-63
    • Jap, B.K.1    Downing, K.H.2    Walian, P.J.3
  • 91
    • 0025091681 scopus 로고
    • Three-dimensional electron diffraction of PhoE porin to 2.8 A resolution
    • Walian P.J., Jap B.K. Three-dimensional electron diffraction of PhoE porin to 2.8 A resolution. J. Mol. Biol. 1990, 215(3):429-438.
    • (1990) J. Mol. Biol. , vol.215 , Issue.3 , pp. 429-438
    • Walian, P.J.1    Jap, B.K.2
  • 92
    • 0029986047 scopus 로고    scopus 로고
    • The micelle to vesicle transition of lipids and detergents in the presence of a membrane protein: Towards a rationale for 2-D crystallization
    • Dolder M., Engel A., Zulauf M. The micelle to vesicle transition of lipids and detergents in the presence of a membrane protein: Towards a rationale for 2-D crystallization. FEBS Lett. 1996, 382(1-2):203-208.
    • (1996) FEBS Lett. , vol.382 , Issue.1-2 , pp. 203-208
    • Dolder, M.1    Engel, A.2    Zulauf, M.3
  • 93
    • 0027155339 scopus 로고
    • Human erythrocyte band 3. Solubilization and reconstitution into two-dimensional crystals
    • Dolder M., Walz T., Hefti A., Engel A. Human erythrocyte band 3. Solubilization and reconstitution into two-dimensional crystals. J. Mol. Biol. 1993, 231(1):119-132.
    • (1993) J. Mol. Biol. , vol.231 , Issue.1 , pp. 119-132
    • Dolder, M.1    Walz, T.2    Hefti, A.3    Engel, A.4
  • 94
    • 0025183233 scopus 로고
    • Ordered arrays of the photosystem I reaction centre after reconstitution: Projections and surface reliefs of the complex at 2 nm resolution
    • Ford R.C., Hefti A., Engel A. Ordered arrays of the photosystem I reaction centre after reconstitution: Projections and surface reliefs of the complex at 2 nm resolution. EMBO J. 1990, 9(10):3067-3075.
    • (1990) EMBO J. , vol.9 , Issue.10 , pp. 3067-3075
    • Ford, R.C.1    Hefti, A.2    Engel, A.3
  • 95
    • 0030949437 scopus 로고    scopus 로고
    • Bio-Beads: An efficient strategy for two-dimensional crystallization of membrane proteins
    • Rigaud J.-L., Mosser G., Lacapere J.-J., Olofsson A., Levy D., Ranck J.-L. Bio-Beads: An efficient strategy for two-dimensional crystallization of membrane proteins. J. Struct. Biol. 1997, 118(3):226-235.
    • (1997) J. Struct. Biol. , vol.118 , Issue.3 , pp. 226-235
    • Rigaud, J.-L.1    Mosser, G.2    Lacapere, J.-J.3    Olofsson, A.4    Levy, D.5    Ranck, J.-L.6
  • 96
    • 0026061928 scopus 로고
    • High-resolution electron crystallography of light-harvesting chlorophyll a/b-protein complex in three different media
    • Wang D.N., Kühlbrandt W. High-resolution electron crystallography of light-harvesting chlorophyll a/b-protein complex in three different media. J. Mol. Biol. 1991, 217(4):691-699.
    • (1991) J. Mol. Biol. , vol.217 , Issue.4 , pp. 691-699
    • Wang, D.N.1    Kühlbrandt, W.2
  • 97
    • 0000095071 scopus 로고
    • Three-dimensional crystals of membrane proteins: Bacteriorhodopsin
    • Michel H., Oesterhelt D. Three-dimensional crystals of membrane proteins: Bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 1980, 77(3):1283-1285.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , Issue.3 , pp. 1283-1285
    • Michel, H.1    Oesterhelt, D.2
  • 98
    • 0032032913 scopus 로고    scopus 로고
    • Selective detergent-extraction from mixed detergent/lipid/protein micelles, using cyclodextrin inclusion compounds: A novel generic approach for the preparation of proteoliposomes
    • Degrip W.J., Vanoostrum J., Bovee-Geurts P.H. Selective detergent-extraction from mixed detergent/lipid/protein micelles, using cyclodextrin inclusion compounds: A novel generic approach for the preparation of proteoliposomes. Biochem. J. 1998, 330(Pt 2):667-674.
    • (1998) Biochem. J. , vol.330 , Issue.PT 2 , pp. 667-674
    • Degrip, W.J.1    Vanoostrum, J.2    Bovee-Geurts, P.H.3
  • 101
    • 33846219153 scopus 로고    scopus 로고
    • Controlled 2-D crystallization of membrane proteins using methyl-beta-cyclodextrin
    • Signorell G.A., Kaufmann T.C., KGBRulski W., Engel A., Remigy H.W. Controlled 2-D crystallization of membrane proteins using methyl-beta-cyclodextrin. J. Struct. Biol. 2007, 157(2):321-328.
    • (2007) J. Struct. Biol. , vol.157 , Issue.2 , pp. 321-328
    • Signorell, G.A.1    Kaufmann, T.C.2    KGBRulski, W.3    Engel, A.4    Remigy, H.W.5
  • 102
    • 0032853933 scopus 로고    scopus 로고
    • Two-dimensional crystallization on lipid layer: A successful approach for membrane proteins
    • Levy D., Mosser G., Lambert O., Moeck G.S., Bald D., Rigaud J.L. Two-dimensional crystallization on lipid layer: A successful approach for membrane proteins. J. Struct. Biol. 1999, 127(1):44-52.
    • (1999) J. Struct. Biol. , vol.127 , Issue.1 , pp. 44-52
    • Levy, D.1    Mosser, G.2    Lambert, O.3    Moeck, G.S.4    Bald, D.5    Rigaud, J.L.6
  • 103
    • 0028590161 scopus 로고
    • Two-dimensional crystallization of histidine-tagged, HIV-1 reverse transcriptase promoted by a novel nickel-chelating lipid
    • Kubalek E.W., Le Grice S.F., Brown P.O. Two-dimensional crystallization of histidine-tagged, HIV-1 reverse transcriptase promoted by a novel nickel-chelating lipid. J. Struct. Biol. 1994, 113(2):117-123.
    • (1994) J. Struct. Biol. , vol.113 , Issue.2 , pp. 117-123
    • Kubalek, E.W.1    Le Grice, S.F.2    Brown, P.O.3
  • 104
    • 0028150044 scopus 로고
    • Synthesis and characterization of chelator-lipids for reversible immobilization of engineered proteins at self-assembled lipid interfaces
    • Schmitt L., Dietrich C., Tampe R. Synthesis and characterization of chelator-lipids for reversible immobilization of engineered proteins at self-assembled lipid interfaces. J. Am. Chem. Soc. 1994, 116:8485-8491.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 8485-8491
    • Schmitt, L.1    Dietrich, C.2    Tampe, R.3
  • 107
    • 33646835810 scopus 로고
    • A negative staining method for high resolution electron microscopy of viruses
    • Brenner S., Horne R.W. A negative staining method for high resolution electron microscopy of viruses. Biochim. Biophys. Acta 1959, 34:103-110.
    • (1959) Biochim. Biophys. Acta , vol.34 , pp. 103-110
    • Brenner, S.1    Horne, R.W.2
  • 110
    • 0016391518 scopus 로고
    • Electron diffraction of frozen, hydrated protein crystals
    • Taylor K.A., Glaeser R.M. Electron diffraction of frozen, hydrated protein crystals. Science 1974, 186(4168):1036-1037.
    • (1974) Science , vol.186 , Issue.4168 , pp. 1036-1037
    • Taylor, K.A.1    Glaeser, R.M.2
  • 113
    • 0034333321 scopus 로고    scopus 로고
    • Parameters affecting specimen flatness of two-dimensional crystals for electron crystallography
    • Vonck J. Parameters affecting specimen flatness of two-dimensional crystals for electron crystallography. Ultramicroscopy 2000, 85(3):123-129.
    • (2000) Ultramicroscopy , vol.85 , Issue.3 , pp. 123-129
    • Vonck, J.1
  • 114
    • 84882752273 scopus 로고
    • In Films That Wet Without Glow Discharge, 35th EMSA Meeting, Louisville, San Francisco Press: Louisville
    • Wall, J. S.; Hainfeld, J. F.; Chung, K. D. In Films That Wet Without Glow Discharge, 35th EMSA Meeting, Louisville, San Francisco Press: Louisville, 1985.
    • (1985)
    • Wall, J.S.1    Hainfeld, J.F.2    Chung, K.D.3
  • 115
    • 1942521362 scopus 로고    scopus 로고
    • Improved specimen preparation for cryo-electron microscopy using a symmetric carbon sandwich technique
    • Gyobu N., Tani K., Hiroaki Y., Kamegawa A., Mitsuoka K., Fujiyoshi Y. Improved specimen preparation for cryo-electron microscopy using a symmetric carbon sandwich technique. J. Struct. Biol. 2004, 146(3):325-333.
    • (2004) J. Struct. Biol. , vol.146 , Issue.3 , pp. 325-333
    • Gyobu, N.1    Tani, K.2    Hiroaki, Y.3    Kamegawa, A.4    Mitsuoka, K.5    Fujiyoshi, Y.6
  • 116
  • 117
    • 77957245653 scopus 로고    scopus 로고
    • Preparation of 2-D crystals of membrane proteins for high-resolution electron crystallography data collection
    • Abeyrathne P.D., Chami M., Pantelic R.S., Goldie K.N., Stahlberg H. Preparation of 2-D crystals of membrane proteins for high-resolution electron crystallography data collection. Meth. Enzymol. 2010, 481:25-43.
    • (2010) Meth. Enzymol. , vol.481 , pp. 25-43
    • Abeyrathne, P.D.1    Chami, M.2    Pantelic, R.S.3    Goldie, K.N.4    Stahlberg, H.5
  • 118
    • 77957222044 scopus 로고    scopus 로고
    • Radiation damage in electron cryomicroscopy
    • Baker L.A., Rubinstein J. Radiation damage in electron cryomicroscopy. Methods Enzymol. 2010, 481:371-388.
    • (2010) Methods Enzymol. , vol.481 , pp. 371-388
    • Baker, L.A.1    Rubinstein, J.2
  • 119
    • 0026031904 scopus 로고
    • Spot-scan imaging in transmission electron microscopy
    • Downing K.H. Spot-scan imaging in transmission electron microscopy. Science 1991, 251(4989):53-59.
    • (1991) Science , vol.251 , Issue.4989 , pp. 53-59
    • Downing, K.H.1
  • 120
    • 0031877370 scopus 로고    scopus 로고
    • Electron crystallography of two-dimensional crystals of membrane proteins
    • Walz T., Grigorieff N. Electron crystallography of two-dimensional crystals of membrane proteins. J. Struct. Biol. 1998, 121(2):142-161.
    • (1998) J. Struct. Biol. , vol.121 , Issue.2 , pp. 142-161
    • Walz, T.1    Grigorieff, N.2
  • 121
    • 0028569793 scopus 로고
    • Applications of a slow-scan CCD camera in protein electron crystallography
    • Brink J., Chiu W. Applications of a slow-scan CCD camera in protein electron crystallography. J. Struct. Biol. 1994, 113(1):23-34.
    • (1994) J. Struct. Biol. , vol.113 , Issue.1 , pp. 23-34
    • Brink, J.1    Chiu, W.2
  • 122
    • 0039841987 scopus 로고    scopus 로고
    • Accurate recording and measurement of electron diffraction data in structural and difference fourier studies of proteins
    • Downing K.H., Li H. Accurate recording and measurement of electron diffraction data in structural and difference fourier studies of proteins. Microsc. Microanal. 2001, 7(5):407-417.
    • (2001) Microsc. Microanal. , vol.7 , Issue.5 , pp. 407-417
    • Downing, K.H.1    Li, H.2
  • 123
    • 0036229990 scopus 로고    scopus 로고
    • Quantitative comparison of zero-loss and conventional electron diffraction from two-dimensional and thin three-dimensional protein crystals
    • Yonekura K., Maki-Yonekura S., Namba K. Quantitative comparison of zero-loss and conventional electron diffraction from two-dimensional and thin three-dimensional protein crystals. Biophys. J. 2002, 82(5):2784-2797.
    • (2002) Biophys. J. , vol.82 , Issue.5 , pp. 2784-2797
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 124
    • 0031700068 scopus 로고    scopus 로고
    • The structural study of membrane proteins by electron crystallography
    • Fujiyoshi Y. The structural study of membrane proteins by electron crystallography. Adv. Biophys. 1998, 35:25-80.
    • (1998) Adv. Biophys. , vol.35 , pp. 25-80
    • Fujiyoshi, Y.1
  • 125
    • 0032599786 scopus 로고    scopus 로고
    • Performance of a 2k CCD camera designed for electron crystallography at 400 kV
    • Downing K.H., Hendrickson F.M. Performance of a 2k CCD camera designed for electron crystallography at 400 kV. Ultramicroscopy 1999, 75(4):215-233.
    • (1999) Ultramicroscopy , vol.75 , Issue.4 , pp. 215-233
    • Downing, K.H.1    Hendrickson, F.M.2
  • 126
    • 36048997627 scopus 로고    scopus 로고
    • Single particle refinement in electron crystallography: A pilot study
    • Koeck P.J., Purhonen P., Alvang R., Grundberg B., Hebert H. Single particle refinement in electron crystallography: A pilot study. J. Struct. Biol. 2007, 160(3):344-352.
    • (2007) J. Struct. Biol. , vol.160 , Issue.3 , pp. 344-352
    • Koeck, P.J.1    Purhonen, P.2    Alvang, R.3    Grundberg, B.4    Hebert, H.5
  • 127
    • 34548425430 scopus 로고    scopus 로고
    • A maximum-likelihood approach to two-dimensional crystals
    • Zeng X., Stahlberg H., Grigorieff N. A maximum-likelihood approach to two-dimensional crystals. J. Struct. Biol. 2007, 160(3):362-374.
    • (2007) J. Struct. Biol. , vol.160 , Issue.3 , pp. 362-374
    • Zeng, X.1    Stahlberg, H.2    Grigorieff, N.3
  • 129
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R., Baldwin J.M., Ceska T.A., Zemlin F., Beckmann E., Downing K.H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 1990, 213(4):899-929.
    • (1990) J. Mol. Biol. , vol.213 , Issue.4 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 130
    • 33845639652 scopus 로고    scopus 로고
    • The contrast-imaging function for tilted specimens
    • Philippsen A., Engel H.A., Engel A. The contrast-imaging function for tilted specimens. Ultramicroscopy 2007, 107(2-3):202-212.
    • (2007) Ultramicroscopy , vol.107 , Issue.2-3 , pp. 202-212
    • Philippsen, A.1    Engel, H.A.2    Engel, A.3
  • 131
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R., Unwin P.N. Three-dimensional model of purple membrane obtained by electron microscopy. Nature 1975, 257(5521):28-32.
    • (1975) Nature , vol.257 , Issue.5521 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.2
  • 132
    • 0020018227 scopus 로고
    • Three-dimensional structure determination by electron microscopy of two-dimensional crystals
    • Amos L.A., Henderson R., Unwin P.N. Three-dimensional structure determination by electron microscopy of two-dimensional crystals. Prog. Biophys. Mol. Biol. 1982, 39(3):183-231.
    • (1982) Prog. Biophys. Mol. Biol. , vol.39 , Issue.3 , pp. 183-231
    • Amos, L.A.1    Henderson, R.2    Unwin, P.N.3
  • 133
    • 0039507411 scopus 로고
    • Structure of purple membrane from Halobacterium halobium: Recording, measurement and evaluation of electron micrographs at 3.5 Å resolution
    • Henderson R., Baldwin J.M., Downing K.H., Lepault J., Zemlin F. Structure of purple membrane from Halobacterium halobium: Recording, measurement and evaluation of electron micrographs at 3.5 Å resolution. Ultramicroscopy 1986, 19:147-178.
    • (1986) Ultramicroscopy , vol.19 , pp. 147-178
    • Henderson, R.1    Baldwin, J.M.2    Downing, K.H.3    Lepault, J.4    Zemlin, F.5
  • 137
    • 0027554794 scopus 로고
    • SPECTRA: A system for processing electron images of crystals
    • Schmid M.F., Dargahi R., Tam M.W. SPECTRA: A system for processing electron images of crystals. Ultramicroscopy 1993, 48(3):251-264.
    • (1993) Ultramicroscopy , vol.48 , Issue.3 , pp. 251-264
    • Schmid, M.F.1    Dargahi, R.2    Tam, M.W.3
  • 138
    • 0029898061 scopus 로고    scopus 로고
    • A brief description of I.C.E.: The integrated crystallographic environment
    • Hardt S., Wang B., Schmid M.F. A brief description of I.C.E.: The integrated crystallographic environment. J. Struct. Biol. 1996, 116(1):68-70.
    • (1996) J. Struct. Biol. , vol.116 , Issue.1 , pp. 68-70
    • Hardt, S.1    Wang, B.2    Schmid, M.F.3
  • 139
    • 0027112252 scopus 로고
    • CRISP Crystallographic image processing on a personal computer
    • Hovmöller S.CRISP Crystallographic image processing on a personal computer. Ultramicroscopy 1992, 41:121-135.
    • (1992) Ultramicroscopy , vol.41 , pp. 121-135
    • Hovmöller, S.1
  • 140
    • 1842473084 scopus 로고    scopus 로고
    • TRICE - a program for reconstructing 3-D reciprocal space and determining unit-cell parameters
    • Zou X.D., Hovmoller A., Hovmoller S. TRICE - a program for reconstructing 3-D reciprocal space and determining unit-cell parameters. Ultramicroscopy 2004, 98(2-4):187-193.
    • (2004) Ultramicroscopy , vol.98 , Issue.2-4 , pp. 187-193
    • Zou, X.D.1    Hovmoller, A.2    Hovmoller, S.3
  • 141
    • 0027721973 scopus 로고
    • Quantitative electron diffraction - new features in the program system ELD
    • Zou X.D., SGBRharev Y., Hovmöller S. Quantitative electron diffraction - new features in the program system ELD. Ultramicroscopy 1993, 52:436-444.
    • (1993) Ultramicroscopy , vol.52 , pp. 436-444
    • Zou, X.D.1    SGBRharev, Y.2    Hovmöller, S.3
  • 142
    • 36049000626 scopus 로고    scopus 로고
    • 2dx_merge: Data management and merging for 2-D crystal images
    • Gipson B., Zeng X., Stahlberg H. 2dx_merge: Data management and merging for 2-D crystal images. J. Struct. Biol. 2007, 160(3):375-384.
    • (2007) J. Struct. Biol. , vol.160 , Issue.3 , pp. 375-384
    • Gipson, B.1    Zeng, X.2    Stahlberg, H.3
  • 143
    • 49549122658 scopus 로고    scopus 로고
    • 2dx - Automated 3-D structure reconstruction from 2-D crystal data
    • Gipson B., Zeng X., Stahlberg H. 2dx - Automated 3-D structure reconstruction from 2-D crystal data. Microsc. Microanal. 2008, 14(Suppl. 2):1290-1291.
    • (2008) Microsc. Microanal. , vol.14 , Issue.SUPPL. 2 , pp. 1290-1291
    • Gipson, B.1    Zeng, X.2    Stahlberg, H.3
  • 144
    • 33845330614 scopus 로고    scopus 로고
    • 2dx - User-friendly image processing for 2-D crystals
    • Gipson B., Zeng X., Zhang Z., Stahlberg H. 2dx - User-friendly image processing for 2-D crystals. J. Struct. Biol. 2007, 157(1):64-72.
    • (2007) J. Struct. Biol. , vol.157 , Issue.1 , pp. 64-72
    • Gipson, B.1    Zeng, X.2    Zhang, Z.3    Stahlberg, H.4
  • 145
    • 36048969226 scopus 로고    scopus 로고
    • Automatic lattice determination for two-dimensional crystal images
    • Zeng X., Gipson B., Zheng Z.Y., Renault L., Stahlberg H. Automatic lattice determination for two-dimensional crystal images. J. Struct. Biol. 2007, 160(3):353-361.
    • (2007) J. Struct. Biol. , vol.160 , Issue.3 , pp. 353-361
    • Zeng, X.1    Gipson, B.2    Zheng, Z.Y.3    Renault, L.4    Stahlberg, H.5
  • 146
    • 0033605231 scopus 로고    scopus 로고
    • The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: Implication of the charge distribution
    • Mitsuoka K., Hirai T., Murata K., Miyazawa A., Kidera A., Kimura Y., Fujiyoshi Y. The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: Implication of the charge distribution. J. Mol. Biol. 1999, 286(3):861-882.
    • (1999) J. Mol. Biol. , vol.286 , Issue.3 , pp. 861-882
    • Mitsuoka, K.1    Hirai, T.2    Murata, K.3    Miyazawa, A.4    Kidera, A.5    Kimura, Y.6    Fujiyoshi, Y.7
  • 148
    • 0344552378 scopus 로고    scopus 로고
    • Iplt - image processing library and toolkit for the electron microscopy community
    • Philippsen A., Schenk A.D., Stahlberg H., Engel A. Iplt - image processing library and toolkit for the electron microscopy community. J. Struct. Biol. 2003, 144(1-2):4-12.
    • (2003) J. Struct. Biol. , vol.144 , Issue.1-2 , pp. 4-12
    • Philippsen, A.1    Schenk, A.D.2    Stahlberg, H.3    Engel, A.4
  • 149
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt W., Wang D.N., Fujiyoshi Y. Atomic model of plant light-harvesting complex by electron crystallography. Nature 1994, 367(6464):614-621.
    • (1994) Nature , vol.367 , Issue.6464 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 150
    • 0035852730 scopus 로고    scopus 로고
    • Visualization of a water-selective pore by electron crystallography in vitreous ice
    • Ren G., Reddy V.S., Cheng A., Melnyk P., Mitra A.K. Visualization of a water-selective pore by electron crystallography in vitreous ice. Proc. Natl. Acad. Sci. USA 2001, 98(4):1398-1403.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.4 , pp. 1398-1403
    • Ren, G.1    Reddy, V.S.2    Cheng, A.3    Melnyk, P.4    Mitra, A.K.5
  • 151
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa A., Fujiyoshi Y., Unwin N. Structure and gating mechanism of the acetylcholine receptor pore. Nature 2003, 424(6943):949-955.
    • (2003) Nature , vol.424 , Issue.6943 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 152
    • 2442659197 scopus 로고    scopus 로고
    • Aquaporin-0 membrane junctions reveal the structure of a closed water pore
    • Gonen T., Sliz P., Kistler J., Cheng Y., Walz T. Aquaporin-0 membrane junctions reveal the structure of a closed water pore. Nature 2004, 429(6988):193-197.
    • (2004) Nature , vol.429 , Issue.6988 , pp. 193-197
    • Gonen, T.1    Sliz, P.2    Kistler, J.3    Cheng, Y.4    Walz, T.5
  • 156
    • 78651359806 scopus 로고    scopus 로고
    • Conformational rearrangement of gastric H(+),K(+)-ATPase induced by an acid suppressant
    • Abe K., Tani K., Fujiyoshi Y. Conformational rearrangement of gastric H(+),K(+)-ATPase induced by an acid suppressant. Nat. Commun. 2011, 2(1):155.
    • (2011) Nat. Commun. , vol.2 , Issue.1 , pp. 155
    • Abe, K.1    Tani, K.2    Fujiyoshi, Y.3
  • 157
    • 3142655417 scopus 로고    scopus 로고
    • Realizing the potential of electron cryo-microscopy
    • Henderson R. Realizing the potential of electron cryo-microscopy. Quart. Rev. Biophys. 2004, 37(1):3-13.
    • (2004) Quart. Rev. Biophys. , vol.37 , Issue.1 , pp. 3-13
    • Henderson, R.1
  • 159
    • 33750378835 scopus 로고    scopus 로고
    • Quasi-symmetry in the cryo-EM structure of EmrE provides the key to modeling its transmembrane domain
    • Fleishman S.J., Harrington S.E., Enosh A., Halperin D., Tate C.G., Ben-Tal N. Quasi-symmetry in the cryo-EM structure of EmrE provides the key to modeling its transmembrane domain. J. Mol. Biol. 2006, 364(1):54-67.
    • (2006) J. Mol. Biol. , vol.364 , Issue.1 , pp. 54-67
    • Fleishman, S.J.1    Harrington, S.E.2    Enosh, A.3    Halperin, D.4    Tate, C.G.5    Ben-Tal, N.6
  • 162
    • 0345543722 scopus 로고    scopus 로고
    • A hexameric transmembrane pore revealed by two-dimensional crystallization of the large mechanosensitive ion channel (MscL) of Escherichia coli
    • Saint N., Lacapere J.J., Gu L.Q., Ghazi A., Martinac B., Rigaud J.L. A hexameric transmembrane pore revealed by two-dimensional crystallization of the large mechanosensitive ion channel (MscL) of Escherichia coli. J. Biol. Chem. 1998, 273(24):14667-14670.
    • (1998) J. Biol. Chem. , vol.273 , Issue.24 , pp. 14667-14670
    • Saint, N.1    Lacapere, J.J.2    Gu, L.Q.3    Ghazi, A.4    Martinac, B.5    Rigaud, J.L.6
  • 163
    • 34249696578 scopus 로고    scopus 로고
    • The supramolecular assemblies of voltage-dependent anion channels in the native membrane
    • Hoogenboom B.W., Suda K., Engel A., Fotiadis D. The supramolecular assemblies of voltage-dependent anion channels in the native membrane. J. Mol. Biol. 2007, 370(2):246-255.
    • (2007) J. Mol. Biol. , vol.370 , Issue.2 , pp. 246-255
    • Hoogenboom, B.W.1    Suda, K.2    Engel, A.3    Fotiadis, D.4
  • 164
    • 0032544651 scopus 로고    scopus 로고
    • Walian, P. J.; Wu, C. L.; Chandy, K. G.; Jap, B. K. Two-dimensional crystallization and projection structure of KcsA potassium channel
    • Li H.L., Sui H.X., Ghanshani S., Lee S. Walian, P. J.; Wu, C. L.; Chandy, K. G.; Jap, B. K. Two-dimensional crystallization and projection structure of KcsA potassium channel. J. Mol. Biol. 1998, 282(2):211-216.
    • (1998) J. Mol. Biol. , vol.282 , Issue.2 , pp. 211-216
    • Li, H.L.1    Sui, H.X.2    Ghanshani, S.3    Lee, S.4
  • 165
    • 26444584556 scopus 로고    scopus 로고
    • Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography
    • Kuo A., Domene C., Johnson L.N., Doyle D.A., Venien-Bryan C. Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography. Structure 2005, 13(10):1463-1472.
    • (2005) Structure , vol.13 , Issue.10 , pp. 1463-1472
    • Kuo, A.1    Domene, C.2    Johnson, L.N.3    Doyle, D.A.4    Venien-Bryan, C.5
  • 166
    • 34548402962 scopus 로고    scopus 로고
    • The structure of the prokaryotic cyclic nucleotide-modulated potassium channel MloK1 at 16 A resolution
    • Chiu P.L., Pagel M.D., Evans J., Chou H.T., Zeng X., Gipson B., Stahlberg H., Nimigean C.M. The structure of the prokaryotic cyclic nucleotide-modulated potassium channel MloK1 at 16 A resolution. Structure 2007, 15(9):1053-1064.
    • (2007) Structure , vol.15 , Issue.9 , pp. 1053-1064
    • Chiu, P.L.1    Pagel, M.D.2    Evans, J.3    Chou, H.T.4    Zeng, X.5    Gipson, B.6    Stahlberg, H.7    Nimigean, C.M.8
  • 167
    • 0035843079 scopus 로고    scopus 로고
    • Projection structure of a ClC-type chloride channel at 6.5 A resolution
    • Mindell J.A., Maduke M., Miller C., Grigorieff N. Projection structure of a ClC-type chloride channel at 6.5 A resolution. Nature 2001, 409(6817):219-223.
    • (2001) Nature , vol.409 , Issue.6817 , pp. 219-223
    • Mindell, J.A.1    Maduke, M.2    Miller, C.3    Grigorieff, N.4
  • 168
    • 59149083869 scopus 로고    scopus 로고
    • Conformations of NhaA, the Na/H exchanger from Escherichia coli, in the pH-activated and ion-translocating states
    • Appel M., Hizlan D., Vinothkumar K.R., Ziegler C., Kühlbrandt W. Conformations of NhaA, the Na/H exchanger from Escherichia coli, in the pH-activated and ion-translocating states. J. Mol. Biol. 2009, 386(2):351-365.
    • (2009) J. Mol. Biol. , vol.386 , Issue.2 , pp. 351-365
    • Appel, M.1    Hizlan, D.2    Vinothkumar, K.R.3    Ziegler, C.4    Kühlbrandt, W.5
  • 169
    • 23844530639 scopus 로고    scopus 로고
    • PH-induced structural change in a sodium/proton antiporter from Methanococcus jannaschii
    • Vinothkumar K.R., Smits S.H., Kühlbrandt W. pH-induced structural change in a sodium/proton antiporter from Methanococcus jannaschii. EMBO J. 2005, 24(15):2720-2729.
    • (2005) EMBO J. , vol.24 , Issue.15 , pp. 2720-2729
    • Vinothkumar, K.R.1    Smits, S.H.2    Kühlbrandt, W.3
  • 170
    • 0032148365 scopus 로고    scopus 로고
    • 7.4-A projection structure of outer membrane phospholipase A from Escherichia coli by electron crystallography
    • Boekema E.J., Stuart M., Koning R.I., Keegstra W., Brisson A., Verheij H.M., Dekker N.A 7.4-A projection structure of outer membrane phospholipase A from Escherichia coli by electron crystallography. J. Struct. Biol. 1998, 123(1):67-71.
    • (1998) J. Struct. Biol. , vol.123 , Issue.1 , pp. 67-71
    • Boekema, E.J.1    Stuart, M.2    Koning, R.I.3    Keegstra, W.4    Brisson, A.5    Verheij, H.M.6    Dekker, N.A.7
  • 172
    • 0035881496 scopus 로고    scopus 로고
    • Projection structure and molecular architecture of OxlT, a bacterial membrane transporter
    • Heymann J.A., Sarker R., Hirai T., Shi D., Milne J.L., Maloney P.C., Subramaniam S. Projection structure and molecular architecture of OxlT, a bacterial membrane transporter. EMBO J. 2001, 20(16):4408-4413.
    • (2001) EMBO J. , vol.20 , Issue.16 , pp. 4408-4413
    • Heymann, J.A.1    Sarker, R.2    Hirai, T.3    Shi, D.4    Milne, J.L.5    Maloney, P.C.6    Subramaniam, S.7
  • 174
    • 1842418729 scopus 로고    scopus 로고
    • Projection structure and oligomeric state of the osmoregulated sodium/glycine betaine symporter BetP of Corynebacterium glutamicum
    • Ziegler C., Morbach S., Schiller D., Kramer R., Tziatzios C., Schubert D., Kühlbrandt W. Projection structure and oligomeric state of the osmoregulated sodium/glycine betaine symporter BetP of Corynebacterium glutamicum. J. Mol. Biol. 2004, 337(5):1137-1147.
    • (2004) J. Mol. Biol. , vol.337 , Issue.5 , pp. 1137-1147
    • Ziegler, C.1    Morbach, S.2    Schiller, D.3    Kramer, R.4    Tziatzios, C.5    Schubert, D.6    Kühlbrandt, W.7
  • 175
    • 33644867700 scopus 로고    scopus 로고
    • Projection structure of the human copper transporter CTR1 at 6-A resolution reveals a compact trimer with a novel channel-like architecture
    • Aller S.G., Unger V.M. Projection structure of the human copper transporter CTR1 at 6-A resolution reveals a compact trimer with a novel channel-like architecture. Proc. Natl. Acad. Sci. USA 2006, 103(10):3627-3632.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.10 , pp. 3627-3632
    • Aller, S.G.1    Unger, V.M.2
  • 177
    • 0037099487 scopus 로고    scopus 로고
    • Projection structure at 8 Å resolution of the melibiose permease, an Na-sugar co-transporter from Escherichia coli
    • Hacksell I., Rigaud J.L., Purhonen P., Pourcher T., Hebert H., Leblanc G. Projection structure at 8 Å resolution of the melibiose permease, an Na-sugar co-transporter from Escherichia coli. EMBO J. 2002, 21(14):3569-3574.
    • (2002) EMBO J. , vol.21 , Issue.14 , pp. 3569-3574
    • Hacksell, I.1    Rigaud, J.L.2    Purhonen, P.3    Pourcher, T.4    Hebert, H.5    Leblanc, G.6
  • 178
    • 77949321417 scopus 로고    scopus 로고
    • +/galactose symporter GalP assembles into functional trimers
    • +/galactose symporter GalP assembles into functional trimers. J. Mol. Biol. 2010, 396(3):593-601.
    • (2010) J. Mol. Biol. , vol.396 , Issue.3 , pp. 593-601
    • Zheng, H.1    Taraska, J.2    Merz, A.J.3    Gonen, T.4
  • 181
    • 58849103158 scopus 로고    scopus 로고
    • Nucleotide dependent packing differences in helical crystals of the ABC transporter MsbA
    • Ward A., Mulligan S., Carragher B., Chang G., Milligan R.A. Nucleotide dependent packing differences in helical crystals of the ABC transporter MsbA. J. Struct. Biol. 2009, 165(3):169-175.
    • (2009) J. Struct. Biol. , vol.165 , Issue.3 , pp. 169-175
    • Ward, A.1    Mulligan, S.2    Carragher, B.3    Chang, G.4    Milligan, R.A.5
  • 182
    • 0035863057 scopus 로고    scopus 로고
    • The projection structure of EmrE, a proton-linked multidrug transporter from Escherichia coli, at 7 A resolution
    • Tate C.G., Kunji E.R., Lebendiker M., Schuldiner S. The projection structure of EmrE, a proton-linked multidrug transporter from Escherichia coli, at 7 A resolution. EMBO J. 2001, 20(1-2):77-81.
    • (2001) EMBO J. , vol.20 , Issue.1-2 , pp. 77-81
    • Tate, C.G.1    Kunji, E.R.2    Lebendiker, M.3    Schuldiner, S.4
  • 183
    • 0041735000 scopus 로고    scopus 로고
    • Conformational changes in the multidrug transporter EmrE associated with substrate binding
    • Tate C.G., Ubarretxena-Belandia I., Baldwin J.M. Conformational changes in the multidrug transporter EmrE associated with substrate binding. J. Mol. Biol. 2003, 332(1):229-242.
    • (2003) J. Mol. Biol. , vol.332 , Issue.1 , pp. 229-242
    • Tate, C.G.1    Ubarretxena-Belandia, I.2    Baldwin, J.M.3
  • 184
    • 0346874401 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer
    • Ubarretxena-Belandia I., Baldwin J.M., Schuldiner S., Tate C.G. Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer. EMBO J. 2003, 22(23):6175-6181.
    • (2003) EMBO J. , vol.22 , Issue.23 , pp. 6175-6181
    • Ubarretxena-Belandia, I.1    Baldwin, J.M.2    Schuldiner, S.3    Tate, C.G.4
  • 185
    • 40849112802 scopus 로고    scopus 로고
    • Electron crystallography reveals plasticity within the drug binding site of the small multidrug transporter EmrE
    • Korkhov V.M., Tate C.G. Electron crystallography reveals plasticity within the drug binding site of the small multidrug transporter EmrE. J. Mol. Biol 2008, 377(4):1094-1103.
    • (2008) J. Mol. Biol , vol.377 , Issue.4 , pp. 1094-1103
    • Korkhov, V.M.1    Tate, C.G.2
  • 186
    • 39749094439 scopus 로고    scopus 로고
    • Conformational change induced by ATP binding in the multidrug ATP-binding cassette transporter BmrA
    • Orelle C., Gubellini F., Durand A., Marco S., Levy D., Gros P., Di Pietro A., Jault J.M. Conformational change induced by ATP binding in the multidrug ATP-binding cassette transporter BmrA. Biochemistry 2008, 47(8):2404-2412.
    • (2008) Biochemistry , vol.47 , Issue.8 , pp. 2404-2412
    • Orelle, C.1    Gubellini, F.2    Durand, A.3    Marco, S.4    Levy, D.5    Gros, P.6    Di Pietro, A.7    Jault, J.M.8
  • 187
    • 0037131184 scopus 로고    scopus 로고
    • Projection structure of P-glycoprotein by electron microscopy. Evidence for a closed conformation of the nucleotide binding domains
    • Lee J.Y., Urbatsch I.L., Senior A.E., Wilkens S. Projection structure of P-glycoprotein by electron microscopy. Evidence for a closed conformation of the nucleotide binding domains. J. Biol. Chem. 2002, 277(42):40125-40131.
    • (2002) J. Biol. Chem. , vol.277 , Issue.42 , pp. 40125-40131
    • Lee, J.Y.1    Urbatsch, I.L.2    Senior, A.E.3    Wilkens, S.4
  • 188
    • 0028339981 scopus 로고
    • Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3
    • Wang D.N., Sarabia V.E., Reithmeier R.A., Kühlbrandt W. Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3. EMBO J. 1994, 13(14):3230-3235.
    • (1994) EMBO J. , vol.13 , Issue.14 , pp. 3230-3235
    • Wang, D.N.1    Sarabia, V.E.2    Reithmeier, R.A.3    Kühlbrandt, W.4
  • 189
    • 77249153631 scopus 로고    scopus 로고
    • Structure of the membrane domain of human erythrocyte anion exchanger 1 revealed by electron crystallography
    • Yamaguchi T., Ikeda Y., Abe Y., Kuma H., Kang D., Hamasaki N., Hirai T. Structure of the membrane domain of human erythrocyte anion exchanger 1 revealed by electron crystallography. J. Mol. Biol. 2010, 397(1):179-189.
    • (2010) J. Mol. Biol. , vol.397 , Issue.1 , pp. 179-189
    • Yamaguchi, T.1    Ikeda, Y.2    Abe, Y.3    Kuma, H.4    Kang, D.5    Hamasaki, N.6    Hirai, T.7
  • 190
    • 0032546752 scopus 로고    scopus 로고
    • Purified lens major intrinsic protein (MIP) forms highly ordered tetragonal two-dimensional arrays by reconstitution
    • Hasler L., Walz T., Tittmann P., Gross H., Kistler J., Engel A. Purified lens major intrinsic protein (MIP) forms highly ordered tetragonal two-dimensional arrays by reconstitution. J. Mol. Biol. 1998, 279(4):855-864.
    • (1998) J. Mol. Biol. , vol.279 , Issue.4 , pp. 855-864
    • Hasler, L.1    Walz, T.2    Tittmann, P.3    Gross, H.4    Kistler, J.5    Engel, A.6
  • 191
    • 4444382267 scopus 로고    scopus 로고
    • Aquaporin-0 membrane junctions form upon proteolytic cleavage
    • Gonen T., Cheng Y., Kistler J., Walz T. Aquaporin-0 membrane junctions form upon proteolytic cleavage. J. Mol. Biol. 2004, 342(4):1337-1345.
    • (2004) J. Mol. Biol. , vol.342 , Issue.4 , pp. 1337-1345
    • Gonen, T.1    Cheng, Y.2    Kistler, J.3    Walz, T.4
  • 193
    • 0034636971 scopus 로고    scopus 로고
    • Three-dimensional fold of the human AQP1 water channel determined at 4 A resolution by electron crystallography of two-dimensional crystals embedded in ice
    • Ren G., Cheng A., Reddy V., Melnyk P., Mitra A.K. Three-dimensional fold of the human AQP1 water channel determined at 4 A resolution by electron crystallography of two-dimensional crystals embedded in ice. J. Mol. Biol. 2000, 301(2):369-387.
    • (2000) J. Mol. Biol. , vol.301 , Issue.2 , pp. 369-387
    • Ren, G.1    Cheng, A.2    Reddy, V.3    Melnyk, P.4    Mitra, A.K.5
  • 194
    • 0029647451 scopus 로고
    • 2O-channel, AQP-CHIP, in projection at 3.5 A resolution
    • 2O-channel, AQP-CHIP, in projection at 3.5 A resolution. J. Mol. Biol. 1995, 251(3):413-420.
    • (1995) J. Mol. Biol. , vol.251 , Issue.3 , pp. 413-420
    • Jap, B.K.1    Li, H.2
  • 195
    • 0035979744 scopus 로고    scopus 로고
    • A refined structure of human aquaporin-1
    • de Groot B.L., Engel A., Grubmüller H. A refined structure of human aquaporin-1. FEBS Lett. 2001, 504(3):206-211.
    • (2001) FEBS Lett. , vol.504 , Issue.3 , pp. 206-211
    • de Groot, B.L.1    Engel, A.2    Grubmüller, H.3
  • 199
    • 0033520347 scopus 로고    scopus 로고
    • Structure of the water channel AqpZ from Escherichia coli revealed by electron crystallography
    • Ringler P., Borgnia M.J., Stahlberg H., Maloney P.C., Agre P., Engel A. Structure of the water channel AqpZ from Escherichia coli revealed by electron crystallography. J. Mol. Biol. 1999, 291(5):1181-1190.
    • (1999) J. Mol. Biol. , vol.291 , Issue.5 , pp. 1181-1190
    • Ringler, P.1    Borgnia, M.J.2    Stahlberg, H.3    Maloney, P.C.4    Agre, P.5    Engel, A.6
  • 201
    • 0035910555 scopus 로고    scopus 로고
    • Structural characterization of two aquaporins isolated from native spinach leaf plasma membranes
    • Fotiadis D., Jeno P., Mini T., Wirtz S., Müller S.A., Fraysse L., Kjellbom P., Engel A. Structural characterization of two aquaporins isolated from native spinach leaf plasma membranes. J. Biol. Chem. 2001, 276(3):1707-1714.
    • (2001) J. Biol. Chem. , vol.276 , Issue.3 , pp. 1707-1714
    • Fotiadis, D.1    Jeno, P.2    Mini, T.3    Wirtz, S.4    Müller, S.A.5    Fraysse, L.6    Kjellbom, P.7    Engel, A.8
  • 202
    • 0033579547 scopus 로고    scopus 로고
    • Projection structure of a plant vacuole membrane aquaporin by electron cryo-crystallography
    • Daniels M.J., Chrispeels M.J., Yeager M. Projection structure of a plant vacuole membrane aquaporin by electron cryo-crystallography. J. Mol. Biol. 1999, 294(5):1337-1349.
    • (1999) J. Mol. Biol. , vol.294 , Issue.5 , pp. 1337-1349
    • Daniels, M.J.1    Chrispeels, M.J.2    Yeager, M.3
  • 205
    • 0021930295 scopus 로고
    • Quaternary structure of the acetylcholine receptor
    • Brisson A., Unwin P.N. Quaternary structure of the acetylcholine receptor. Nature 1985, 315(6019):474-477.
    • (1985) Nature , vol.315 , Issue.6019 , pp. 474-477
    • Brisson, A.1    Unwin, P.N.2
  • 206
    • 0024290709 scopus 로고
    • Ion channel of acetylcholine receptor reconstructed from images of postsynaptic membranes
    • Toyoshima C., Unwin N. Ion channel of acetylcholine receptor reconstructed from images of postsynaptic membranes. Nature 1988, 336(6196):247-250.
    • (1988) Nature , vol.336 , Issue.6196 , pp. 247-250
    • Toyoshima, C.1    Unwin, N.2
  • 207
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin N. Acetylcholine receptor channel imaged in the open state. Nature 1995, 373(6509):37-43.
    • (1995) Nature , vol.373 , Issue.6509 , pp. 37-43
    • Unwin, N.1
  • 209
    • 77953560009 scopus 로고    scopus 로고
    • Three-dimensional structure of TspO by electron cryomicroscopy of helical crystals
    • Korkhov V.M., Sachse C., Short J.M., Tate C.G. Three-dimensional structure of TspO by electron cryomicroscopy of helical crystals. Structure 2010, 18(6):677-687.
    • (2010) Structure , vol.18 , Issue.6 , pp. 677-687
    • Korkhov, V.M.1    Sachse, C.2    Short, J.M.3    Tate, C.G.4
  • 210
    • 0035979743 scopus 로고    scopus 로고
    • Two-dimensional crystallization of membrane proteins: The lipid layer strategy
    • Levy D., Chami M., Rigaud J.L. Two-dimensional crystallization of membrane proteins: The lipid layer strategy. FEBS Lett. 2001, 504(3):187-193.
    • (2001) FEBS Lett. , vol.504 , Issue.3 , pp. 187-193
    • Levy, D.1    Chami, M.2    Rigaud, J.L.3
  • 211
    • 33846235560 scopus 로고    scopus 로고
    • Two-dimensional crystallization of human vitamin K-dependent gamma-glutamyl carboxylase
    • Schmidt-Krey I., Haase W., Mutucumarana V., Stafford D.W., Kühlbrandt W. Two-dimensional crystallization of human vitamin K-dependent gamma-glutamyl carboxylase. J. Struct. Biol. 2007, 157(2):437-442.
    • (2007) J. Struct. Biol. , vol.157 , Issue.2 , pp. 437-442
    • Schmidt-Krey, I.1    Haase, W.2    Mutucumarana, V.3    Stafford, D.W.4    Kühlbrandt, W.5
  • 212
    • 0020536327 scopus 로고
    • Three-dimensional structure of orthorhombic purple membrane at 6.5 A resolution
    • Leifer D., Henderson R. Three-dimensional structure of orthorhombic purple membrane at 6.5 A resolution. J. Mol. Biol. 1983, 163(3):451-466.
    • (1983) J. Mol. Biol. , vol.163 , Issue.3 , pp. 451-466
    • Leifer, D.1    Henderson, R.2
  • 213
    • 0011197760 scopus 로고
    • Three-dimensional structure of deoxycholate-treated purple membrane at 6Å resolution and molecular averaging of three crystal forms of bacteriorhodopsin
    • Tsygannik I.N., Baldwin J.M. Three-dimensional structure of deoxycholate-treated purple membrane at 6Å resolution and molecular averaging of three crystal forms of bacteriorhodopsin. Eur. Biophys. J. 1987, 14(5):263-272.
    • (1987) Eur. Biophys. J. , vol.14 , Issue.5 , pp. 263-272
    • Tsygannik, I.N.1    Baldwin, J.M.2
  • 214
    • 0029903197 scopus 로고    scopus 로고
    • Electron-crystallographic refinement of the structure of bacteriorhodopsin
    • Grigorieff N., Ceska T.A., Downing K.H., Baldwin J.M., Henderson R. Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 1996, 259(3):393-421.
    • (1996) J. Mol. Biol. , vol.259 , Issue.3 , pp. 393-421
    • Grigorieff, N.1    Ceska, T.A.2    Downing, K.H.3    Baldwin, J.M.4    Henderson, R.5
  • 216
    • 0033548544 scopus 로고    scopus 로고
    • The projection structure of the low temperature K intermediate of the bacteriorhodopsin photocycle determined by electron diffraction
    • Bullough P.A., Henderson R. The projection structure of the low temperature K intermediate of the bacteriorhodopsin photocycle determined by electron diffraction. J. Mol. Biol. 1999, 286(5):1663-1671.
    • (1999) J. Mol. Biol. , vol.286 , Issue.5 , pp. 1663-1671
    • Bullough, P.A.1    Henderson, R.2
  • 218
    • 0034632864 scopus 로고    scopus 로고
    • Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
    • Subramaniam S., Henderson R. Molecular mechanism of vectorial proton translocation by bacteriorhodopsin. Nature 2000, 406(6796):653-657.
    • (2000) Nature , vol.406 , Issue.6796 , pp. 653-657
    • Subramaniam, S.1    Henderson, R.2
  • 219
    • 0034658269 scopus 로고    scopus 로고
    • Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography
    • Vonck J. Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography. EMBO J. 2000, 19(10):2152-2160.
    • (2000) EMBO J. , vol.19 , Issue.10 , pp. 2152-2160
    • Vonck, J.1
  • 220
    • 0021582830 scopus 로고
    • Measurement and evaluation of electron diffraction patterns from two-dimensional crystals
    • Baldwin J., Henderson R. Measurement and evaluation of electron diffraction patterns from two-dimensional crystals. Ultramicroscopy 1984, 14(4):319-335.
    • (1984) Ultramicroscopy , vol.14 , Issue.4 , pp. 319-335
    • Baldwin, J.1    Henderson, R.2
  • 221
    • 0027144770 scopus 로고
    • Projection structure of halorhodopsin from Halobacterium halobium at 6 A resolution obtained by electron cryo-microscopy
    • Havelka W.A., Henderson R., Heymann J.A., Oesterhelt D. Projection structure of halorhodopsin from Halobacterium halobium at 6 A resolution obtained by electron cryo-microscopy. J. Mol. Biol. 1993, 234(3):837-846.
    • (1993) J. Mol. Biol. , vol.234 , Issue.3 , pp. 837-846
    • Havelka, W.A.1    Henderson, R.2    Heymann, J.A.3    Oesterhelt, D.4
  • 222
    • 0028959025 scopus 로고
    • Three-dimensional structure of halorhodopsin at 7 A resolution
    • Havelka W.A., Henderson R., Oesterhelt D. Three-dimensional structure of halorhodopsin at 7 A resolution. J. Mol. Biol. 1995, 247(4):726-738.
    • (1995) J. Mol. Biol. , vol.247 , Issue.4 , pp. 726-738
    • Havelka, W.A.1    Henderson, R.2    Oesterhelt, D.3
  • 223
    • 0034712851 scopus 로고    scopus 로고
    • The three-dimensional structure of halorhodopsin to 5 Å by electron crystallography: A new unbending procedure for two-dimensional crystals by using a global reference structure
    • Kunji E.R., von Gronau S., Oesterhelt D., Henderson R. The three-dimensional structure of halorhodopsin to 5 Å by electron crystallography: A new unbending procedure for two-dimensional crystals by using a global reference structure. Proc. Natl. Acad. Sci. USA 2000, 97(9):4637-4642.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.9 , pp. 4637-4642
    • Kunji, E.R.1    von Gronau, S.2    Oesterhelt, D.3    Henderson, R.4
  • 224
    • 5044235587 scopus 로고    scopus 로고
    • Electron crystallography reveals the structure of metarhodopsin I
    • Ruprecht J.J., Mielke T., Vogel R., Villa C., Schertler G.F. Electron crystallography reveals the structure of metarhodopsin I. EMBO J. 2004, 23(18):3609-3620.
    • (2004) EMBO J. , vol.23 , Issue.18 , pp. 3609-3620
    • Ruprecht, J.J.1    Mielke, T.2    Vogel, R.3    Villa, C.4    Schertler, G.F.5
  • 225
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • Schertler G.F., Villa C., Henderson R. Projection structure of rhodopsin. Nature 1993, 362(6422):770-772.
    • (1993) Nature , vol.362 , Issue.6422 , pp. 770-772
    • Schertler, G.F.1    Villa, C.2    Henderson, R.3
  • 226
    • 0028962270 scopus 로고
    • Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy
    • Unger V.M., Schertler G.F. Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy. Biophys. J. 1995, 68(5):1776-1786.
    • (1995) Biophys. J. , vol.68 , Issue.5 , pp. 1776-1786
    • Unger, V.M.1    Schertler, G.F.2
  • 227
    • 0032500697 scopus 로고    scopus 로고
    • Characterisation of an improved two-dimensional p22121 crystal from bovine rhodopsin
    • Krebs A., Villa C., Edwards P.C., Schertler G.F. Characterisation of an improved two-dimensional p22121 crystal from bovine rhodopsin. J. Mol. Biol. 1998, 282(5):991-1003.
    • (1998) J. Mol. Biol. , vol.282 , Issue.5 , pp. 991-1003
    • Krebs, A.1    Villa, C.2    Edwards, P.C.3    Schertler, G.F.4
  • 228
    • 0347379900 scopus 로고    scopus 로고
    • The three-dimensional structure of bovine rhodopsin determined by electron cryomicroscopy
    • Krebs A., Edwards P.C., Villa C., Li J., Schertler G.F. The three-dimensional structure of bovine rhodopsin determined by electron cryomicroscopy. J. Biol. Chem. 2003, 278(50):50217-50225.
    • (2003) J. Biol. Chem. , vol.278 , Issue.50 , pp. 50217-50225
    • Krebs, A.1    Edwards, P.C.2    Villa, C.3    Li, J.4    Schertler, G.F.5
  • 230
    • 0035976714 scopus 로고    scopus 로고
    • Three-dimensional structure of an invertebrate rhodopsin and basis for ordered alignment in the photoreceptor membrane
    • Davies A., Gowen B.E., Krebs A.M., Schertler G.F., Saibil H.R. Three-dimensional structure of an invertebrate rhodopsin and basis for ordered alignment in the photoreceptor membrane. J. Mol. Biol. 2001, 314(3):455-463.
    • (2001) J. Mol. Biol. , vol.314 , Issue.3 , pp. 455-463
    • Davies, A.1    Gowen, B.E.2    Krebs, A.M.3    Schertler, G.F.4    Saibil, H.R.5
  • 231
    • 0034006276 scopus 로고    scopus 로고
    • Preparation and analysis of two-dimensional crystals of rhodopsin
    • Schertler G.F., Hargrave P.A. Preparation and analysis of two-dimensional crystals of rhodopsin. Meth. Enzymol. 2000, 315:91-107.
    • (2000) Meth. Enzymol. , vol.315 , pp. 91-107
    • Schertler, G.F.1    Hargrave, P.A.2
  • 232
    • 0035957524 scopus 로고    scopus 로고
    • Electron crystallographic analysis of two-dimensional crystals of sensory rhodopsin II: A 6.9 A projection structure
    • Kunji E.R., Spudich E.N., Grisshammer R., Henderson R., Spudich J.L. Electron crystallographic analysis of two-dimensional crystals of sensory rhodopsin II: A 6.9 A projection structure. J. Mol. Biol. 2001, 308(2):279-293.
    • (2001) J. Mol. Biol. , vol.308 , Issue.2 , pp. 279-293
    • Kunji, E.R.1    Spudich, E.N.2    Grisshammer, R.3    Henderson, R.4    Spudich, J.L.5
  • 233
    • 81055155876 scopus 로고    scopus 로고
    • Projection structure of channelrodopsin-2 at 6A resolution electron crystallography
    • Müller M., Bamann C., Bamberg E., Kühlbrandt W. Projection structure of channelrodopsin-2 at 6A resolution electron crystallography. J. Mol. Biol. 2011, 414(1):86-95.
    • (2011) J. Mol. Biol. , vol.414 , Issue.1 , pp. 86-95
    • Müller, M.1    Bamann, C.2    Bamberg, E.3    Kühlbrandt, W.4
  • 234
    • 0037043724 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacterial protein-translocation complex SecYEG
    • Breyton C., Haase W., Rapoport T.A., Kühlbrandt W., Collinson I. Three-dimensional structure of the bacterial protein-translocation complex SecYEG. Nature 2002, 418(6898):662-665.
    • (2002) Nature , vol.418 , Issue.6898 , pp. 662-665
    • Breyton, C.1    Haase, W.2    Rapoport, T.A.3    Kühlbrandt, W.4    Collinson, I.5
  • 235
    • 37349111755 scopus 로고    scopus 로고
    • Projection structure of yidC: A conserved mediator of membrane protein assembly
    • Lotz M., Haase W., Kühlbrandt W., Collinson I. Projection structure of yidC: A conserved mediator of membrane protein assembly. J. Mol. Biol. 2008, 375(4):901-907.
    • (2008) J. Mol. Biol. , vol.375 , Issue.4 , pp. 901-907
    • Lotz, M.1    Haase, W.2    Kühlbrandt, W.3    Collinson, I.4
  • 236
    • 0031554721 scopus 로고    scopus 로고
    • The 3.0 A projection structure of microsomal glutathione transferase as determined by electron crystallography of p 21212 two-dimensional crystals
    • Hebert H., Schmidt-Krey I., Morgenstern R., Murata K., Hirai T., Mitsuoka K., Fujiyoshi Y. The 3.0 A projection structure of microsomal glutathione transferase as determined by electron crystallography of p 21212 two-dimensional crystals. J. Mol. Biol. 1997, 271(5):751-758.
    • (1997) J. Mol. Biol. , vol.271 , Issue.5 , pp. 751-758
    • Hebert, H.1    Schmidt-Krey, I.2    Morgenstern, R.3    Murata, K.4    Hirai, T.5    Mitsuoka, K.6    Fujiyoshi, Y.7
  • 237
    • 0031763026 scopus 로고    scopus 로고
    • Parameters for the two-dimensional crystallization of the membrane protein microsomal glutathione transferase
    • Schmidt-Krey I., Lundqvist G., Morgenstern R., Hebert H. Parameters for the two-dimensional crystallization of the membrane protein microsomal glutathione transferase. J. Struct. Biol. 1998, 123(2):87-96.
    • (1998) J. Struct. Biol. , vol.123 , Issue.2 , pp. 87-96
    • Schmidt-Krey, I.1    Lundqvist, G.2    Morgenstern, R.3    Hebert, H.4
  • 238
    • 0033617247 scopus 로고    scopus 로고
    • The projection structure of the membrane protein microsomal glutathione transferase at 3 A resolution as determined from two-dimensional hexagonal crystals
    • Schmidt-Krey I., Murata K., Hirai T., Mitsuoka K., Cheng Y., Morgenstern R., Fujiyoshi Y., Hebert H. The projection structure of the membrane protein microsomal glutathione transferase at 3 A resolution as determined from two-dimensional hexagonal crystals. J. Mol. Biol. 1999, 288(2):243-253.
    • (1999) J. Mol. Biol. , vol.288 , Issue.2 , pp. 243-253
    • Schmidt-Krey, I.1    Murata, K.2    Hirai, T.3    Mitsuoka, K.4    Cheng, Y.5    Morgenstern, R.6    Fujiyoshi, Y.7    Hebert, H.8
  • 240
    • 0037060464 scopus 로고    scopus 로고
    • The 3-D structure of microsomal glutathione transferase 1 at 6 A resolution as determined by electron crystallography of p22(1)2(1) crystals
    • Holm P.J., Morgenstern R., Hebert H. The 3-D structure of microsomal glutathione transferase 1 at 6 A resolution as determined by electron crystallography of p22(1)2(1) crystals. Biochim. Biophys. Acta 2002, 1594(2):276-285.
    • (2002) Biochim. Biophys. Acta , vol.1594 , Issue.2 , pp. 276-285
    • Holm, P.J.1    Morgenstern, R.2    Hebert, H.3
  • 242
    • 76749150941 scopus 로고    scopus 로고
    • Two-dimensional crystallization conditions of human leukotriene C4 synthase requiring adjustment of a particularly large combination of specific parameters
    • Zhao G., Johnson M.C., Schnell J.R., Kanaoka Y., Haase W., Irikura D., Lam B.K., Schmidt-Krey I. Two-dimensional crystallization conditions of human leukotriene C4 synthase requiring adjustment of a particularly large combination of specific parameters. J. Struct. Biol. 2010, 169(3):450-454.
    • (2010) J. Struct. Biol. , vol.169 , Issue.3 , pp. 450-454
    • Zhao, G.1    Johnson, M.C.2    Schnell, J.R.3    Kanaoka, Y.4    Haase, W.5    Irikura, D.6    Lam, B.K.7    Schmidt-Krey, I.8
  • 243
    • 0020512745 scopus 로고
    • Two-dimensional crystals formed from photosynthetic reaction centers
    • Miller K.R., Jacob J.S. Two-dimensional crystals formed from photosynthetic reaction centers. J. Cell Biol. 1983, 97(4):1266-1270.
    • (1983) J. Cell Biol. , vol.97 , Issue.4 , pp. 1266-1270
    • Miller, K.R.1    Jacob, J.S.2
  • 244
    • 0028953308 scopus 로고
    • The 8.5 A projection map of the light-harvesting complex I from Rhodospirillum rubrum reveals a ring composed of 16 subunits
    • Karrasch S., Bullough P.A., Ghosh R. The 8.5 A projection map of the light-harvesting complex I from Rhodospirillum rubrum reveals a ring composed of 16 subunits. EMBO J. 1995, 14(4):631-638.
    • (1995) EMBO J. , vol.14 , Issue.4 , pp. 631-638
    • Karrasch, S.1    Bullough, P.A.2    Ghosh, R.3
  • 245
    • 0032475815 scopus 로고    scopus 로고
    • Projection structures of three photosynthetic complexes from Rhodobacter sphaeroides: LH2 at 6 A, LH1 and RC-LH1 at 25A
    • Walz T., Jamieson S.J., Bowers C.M., Bullough P.A., Hunter C.N. Projection structures of three photosynthetic complexes from Rhodobacter sphaeroides: LH2 at 6 A, LH1 and RC-LH1 at 25A. J. Mol. Biol. 1998, 282(4):833-845.
    • (1998) J. Mol. Biol. , vol.282 , Issue.4 , pp. 833-845
    • Walz, T.1    Jamieson, S.J.2    Bowers, C.M.3    Bullough, P.A.4    Hunter, C.N.5
  • 246
    • 0031830394 scopus 로고    scopus 로고
    • The reaction centre of the photounit of Rhodospirillum rubrum is anchored to the light-harvesting complex with four-fold rotational disorder
    • Stahlberg H., Dubochet J., Vogel H., Ghosh R. The reaction centre of the photounit of Rhodospirillum rubrum is anchored to the light-harvesting complex with four-fold rotational disorder. Photosynth. Res. 1998, 55:363-368.
    • (1998) Photosynth. Res. , vol.55 , pp. 363-368
    • Stahlberg, H.1    Dubochet, J.2    Vogel, H.3    Ghosh, R.4
  • 247
    • 0032478682 scopus 로고    scopus 로고
    • Projection map of the reaction center-light harvesting 1 complex from Rhodopseudomonas viridis at 10 A resolution
    • Ikeda-Yamasaki I., Odahara T., Mitsuoka K., Fujiyoshi Y., Murata K. Projection map of the reaction center-light harvesting 1 complex from Rhodopseudomonas viridis at 10 A resolution. FEBS Lett. 1998, 425(3):505-508.
    • (1998) FEBS Lett. , vol.425 , Issue.3 , pp. 505-508
    • Ikeda-Yamasaki, I.1    Odahara, T.2    Mitsuoka, K.3    Fujiyoshi, Y.4    Murata, K.5
  • 248
    • 0036683068 scopus 로고    scopus 로고
    • Projection structure of the photosynthetic reaction centre-antenna complex of Rhodospirillum rubrum at 8.5A resolution
    • Jamieson S.J., Wang P., Qian P., Kirkland J.Y., Conroy M.J., Hunter C.N., Bullough P.A. Projection structure of the photosynthetic reaction centre-antenna complex of Rhodospirillum rubrum at 8.5A resolution. EMBO J. 2002, 21(15):3927-3935.
    • (2002) EMBO J. , vol.21 , Issue.15 , pp. 3927-3935
    • Jamieson, S.J.1    Wang, P.2    Qian, P.3    Kirkland, J.Y.4    Conroy, M.J.5    Hunter, C.N.6    Bullough, P.A.7
  • 249
    • 0037593237 scopus 로고    scopus 로고
    • A reaction center-light-harvesting 1 complex (RC-LH1) from a Rhodospirillum rubrum mutant with altered esterifying pigments: Characterization by optical spectroscopy and cryo-electron microscopy
    • Qian P., Addlesee H.A., Ruban A.V., Wang P., Bullough P.A., Hunter C.N. A reaction center-light-harvesting 1 complex (RC-LH1) from a Rhodospirillum rubrum mutant with altered esterifying pigments: Characterization by optical spectroscopy and cryo-electron microscopy. J. Biol. Chem. 2003, 278(26):23678-23685.
    • (2003) J. Biol. Chem. , vol.278 , Issue.26 , pp. 23678-23685
    • Qian, P.1    Addlesee, H.A.2    Ruban, A.V.3    Wang, P.4    Bullough, P.A.5    Hunter, C.N.6
  • 250
    • 0942287196 scopus 로고    scopus 로고
    • Structural role of PufX in the dimerization of the photosynthetic core complex of Rhodobacter sphaeroides
    • Scheuring S., Francia F., Busselez J., Melandri B.A., Rigaud J.L., Levy D. Structural role of PufX in the dimerization of the photosynthetic core complex of Rhodobacter sphaeroides. J. Biol. Chem. 2004, 279(5):3620-3626.
    • (2004) J. Biol. Chem. , vol.279 , Issue.5 , pp. 3620-3626
    • Scheuring, S.1    Francia, F.2    Busselez, J.3    Melandri, B.A.4    Rigaud, J.L.5    Levy, D.6
  • 251
    • 20344374627 scopus 로고    scopus 로고
    • The 8.5A projection structure of the core RC-LH1-PufX dimer of Rhodobacter sphaeroides
    • Qian P., Hunter C.N., Bullough P.A. The 8.5A projection structure of the core RC-LH1-PufX dimer of Rhodobacter sphaeroides. J. Mol. Biol. 2005, 349(5):948-960.
    • (2005) J. Mol. Biol. , vol.349 , Issue.5 , pp. 948-960
    • Qian, P.1    Hunter, C.N.2    Bullough, P.A.3
  • 252
    • 1842510034 scopus 로고    scopus 로고
    • Molecular architecture of photosynthetic membranes in Rhodobacter sphaeroides: The role of PufX
    • Siebert C.A., Qian P., Fotiadis D., Engel A., Hunter C.N., Bullough P.A. Molecular architecture of photosynthetic membranes in Rhodobacter sphaeroides: The role of PufX. EMBO J. 2004, 23(4):690-700.
    • (2004) EMBO J. , vol.23 , Issue.4 , pp. 690-700
    • Siebert, C.A.1    Qian, P.2    Fotiadis, D.3    Engel, A.4    Hunter, C.N.5    Bullough, P.A.6
  • 253
    • 0029029180 scopus 로고
    • Two-dimensional crystallization and preliminary structure analysis of light harvesting II (B800-850) complex from the purple bacterium Rhodovulum sulfidophilum
    • Montoya G., Cyrklaff M., Sinning I. Two-dimensional crystallization and preliminary structure analysis of light harvesting II (B800-850) complex from the purple bacterium Rhodovulum sulfidophilum. J. Mol. Biol. 1995, 250(1):1-10.
    • (1995) J. Mol. Biol. , vol.250 , Issue.1 , pp. 1-10
    • Montoya, G.1    Cyrklaff, M.2    Sinning, I.3
  • 254
    • 0030584656 scopus 로고    scopus 로고
    • Two-dimensional structure of light harvesting complex II (LHII) from the purple bacterium Rhodovulum sulfidophilum and comparison with LHII from Rhodopseudomonas acidophila
    • Savage H., Cyrklaff M., Montoya G., Kühlbrandt W., Sinning I. Two-dimensional structure of light harvesting complex II (LHII) from the purple bacterium Rhodovulum sulfidophilum and comparison with LHII from Rhodopseudomonas acidophila. Structure 1996, 4(3):243-252.
    • (1996) Structure , vol.4 , Issue.3 , pp. 243-252
    • Savage, H.1    Cyrklaff, M.2    Montoya, G.3    Kühlbrandt, W.4    Sinning, I.5
  • 255
    • 0035796958 scopus 로고    scopus 로고
    • Two-dimensional structure of the native light-harvesting complex LH2 from Rubrivivax gelatinosus and of a truncated form
    • Ranck J., Ruiz T., Pehau-Arnaudet G., Arnoux B., Reiss-Husson F. Two-dimensional structure of the native light-harvesting complex LH2 from Rubrivivax gelatinosus and of a truncated form. Biochim. Biophys. Acta 2001, 1506(1):67-78.
    • (2001) Biochim. Biophys. Acta , vol.1506 , Issue.1 , pp. 67-78
    • Ranck, J.1    Ruiz, T.2    Pehau-Arnaudet, G.3    Arnoux, B.4    Reiss-Husson, F.5
  • 256
    • 0026562059 scopus 로고
    • The structure of photosystem I from the thermophilic cyanobacterium Synechococcus sp. determined by electron microscopy of two-dimensional crystals
    • Böttcher B., Graber P., Boekema E.J. The structure of photosystem I from the thermophilic cyanobacterium Synechococcus sp. determined by electron microscopy of two-dimensional crystals. Biochim. Biophys. Acta 1992, 1100(2):125-136.
    • (1992) Biochim. Biophys. Acta , vol.1100 , Issue.2 , pp. 125-136
    • Böttcher, B.1    Graber, P.2    Boekema, E.J.3
  • 258
    • 0033053334 scopus 로고    scopus 로고
    • Revealing the structure of the oxygen-evolving core dimer of photosystem II by cryoelectron crystallography
    • Hankamer B., Morris E.P., Barber J. Revealing the structure of the oxygen-evolving core dimer of photosystem II by cryoelectron crystallography. Nat. Struct. Biol. 1999, 6(6):560-564.
    • (1999) Nat. Struct. Biol. , vol.6 , Issue.6 , pp. 560-564
    • Hankamer, B.1    Morris, E.P.2    Barber, J.3
  • 259
    • 0037161244 scopus 로고    scopus 로고
    • Electron crystallographic study of photosystem II of the cyanobacterium Synechococcus elongatus
    • da Fonseca P., Morris E.P., Hankamer B., Barber J. Electron crystallographic study of photosystem II of the cyanobacterium Synechococcus elongatus. Biochemistry 2002, 41(16):5163-5167.
    • (2002) Biochemistry , vol.41 , Issue.16 , pp. 5163-5167
    • da Fonseca, P.1    Morris, E.P.2    Hankamer, B.3    Barber, J.4
  • 260
    • 33749373006 scopus 로고    scopus 로고
    • Biochemical and structural analyses of a higher plant photosystem II supercomplex of a photosystem I-less mutant of barley. Consequences of a chronic over-reduction of the plastoquinone pool
    • Morosinotto T., Bassi R., Frigerio S., Finazzi G., Morris E., Barber J. Biochemical and structural analyses of a higher plant photosystem II supercomplex of a photosystem I-less mutant of barley. Consequences of a chronic over-reduction of the plastoquinone pool. FEBS J. 2006, 273(20):4616-4630.
    • (2006) FEBS J. , vol.273 , Issue.20 , pp. 4616-4630
    • Morosinotto, T.1    Bassi, R.2    Frigerio, S.3    Finazzi, G.4    Morris, E.5    Barber, J.6
  • 261
    • 0024974779 scopus 로고
    • Two-dimensional structure of plant light-harvesting complex at 3.7 A [corrected] resolution by electron crystallography
    • Kühlbrandt W., Downing K.H. Two-dimensional structure of plant light-harvesting complex at 3.7 A [corrected] resolution by electron crystallography. J. Mol. Biol. 1989, 207(4):823-828.
    • (1989) J. Mol. Biol. , vol.207 , Issue.4 , pp. 823-828
    • Kühlbrandt, W.1    Downing, K.H.2
  • 262
    • 0025898707 scopus 로고
    • Three-dimensional structure of plant light-harvesting complex determined by electron crystallography
    • Kühlbrandt W., Wang D.N. Three-dimensional structure of plant light-harvesting complex determined by electron crystallography. Nature 1991, 350(6314):130-134.
    • (1991) Nature , vol.350 , Issue.6314 , pp. 130-134
    • Kühlbrandt, W.1    Wang, D.N.2
  • 263
    • 0030060736 scopus 로고    scopus 로고
    • Two-dimensional crystals of LH2 light-harvesting complexes from Ectothiorhodospira sp. and Rhodobacter capsulatus investigated by electron microscopy
    • Oling F., Boekema E.J., Ortiz de Zarate I., Visschers R., van Grondelle R., Keegstra W., Brisson A., Picorel R. Two-dimensional crystals of LH2 light-harvesting complexes from Ectothiorhodospira sp. and Rhodobacter capsulatus investigated by electron microscopy. Biochim. Biophys. Acta 1996, 1273(1):44-50.
    • (1996) Biochim. Biophys. Acta , vol.1273 , Issue.1 , pp. 44-50
    • Oling, F.1    Boekema, E.J.2    Ortiz de Zarate, I.3    Visschers, R.4    van Grondelle, R.5    Keegstra, W.6    Brisson, A.7    Picorel, R.8
  • 264
    • 0030009893 scopus 로고    scopus 로고
    • Three-dimensional structure of bovine cytochrome bc1 complex by electron cryomicroscopy and helical image reconstruction
    • Akiba T., Toyoshima C., Matsunaga T., Kawamoto M., Kubota T., FGBRuyama K., Namba K., Matsubara H. Three-dimensional structure of bovine cytochrome bc1 complex by electron cryomicroscopy and helical image reconstruction. Nat. Struct. Biol. 1996, 3(6):553-561.
    • (1996) Nat. Struct. Biol. , vol.3 , Issue.6 , pp. 553-561
    • Akiba, T.1    Toyoshima, C.2    Matsunaga, T.3    Kawamoto, M.4    Kubota, T.5    FGBRuyama, K.6    Namba, K.7    Matsubara, H.8
  • 265
    • 0030897302 scopus 로고    scopus 로고
    • Projection structure of the cytochrome bo ubiquinol oxidase from Escherichia coli at 6 A resolution
    • Gohlke U., Warne A., Saraste M. Projection structure of the cytochrome bo ubiquinol oxidase from Escherichia coli at 6 A resolution. EMBO J 1997, 16(6):1181-1188.
    • (1997) EMBO J , vol.16 , Issue.6 , pp. 1181-1188
    • Gohlke, U.1    Warne, A.2    Saraste, M.3
  • 266
    • 0017807903 scopus 로고
    • Structure and orientation of cytochrome c oxidase in crystalline membranes. Studies by electron microscopy and by labeling with subunit-specific antibodies
    • Frey T.G., Chan S.H., Schatz G. Structure and orientation of cytochrome c oxidase in crystalline membranes. Studies by electron microscopy and by labeling with subunit-specific antibodies. J. Biol. Chem. 1978, 253(12):4389-4395.
    • (1978) J. Biol. Chem. , vol.253 , Issue.12 , pp. 4389-4395
    • Frey, T.G.1    Chan, S.H.2    Schatz, G.3
  • 267
    • 0028828124 scopus 로고
    • Purification and two-dimensional crystallization of bacterial cytochrome oxidases
    • Warne A., Wang D.N., Saraste M. Purification and two-dimensional crystallization of bacterial cytochrome oxidases. Eur. J. Biochem. 1995, 234(2):443-451.
    • (1995) Eur. J. Biochem. , vol.234 , Issue.2 , pp. 443-451
    • Warne, A.1    Wang, D.N.2    Saraste, M.3
  • 268
    • 0018289428 scopus 로고
    • Membrane crystals of ubiquinone:cytochrome c reductase from Neurospora mitochondria
    • Wingfield P., Arad T., Leonard K., Weiss H. Membrane crystals of ubiquinone:cytochrome c reductase from Neurospora mitochondria. Nature 1979, 280(5724):696-697.
    • (1979) Nature , vol.280 , Issue.5724 , pp. 696-697
    • Wingfield, P.1    Arad, T.2    Leonard, K.3    Weiss, H.4
  • 269
    • 0034665878 scopus 로고    scopus 로고
    • Cryo-electron crystallography of two sub-complexes of bovine complex I reveals the relationship between the membrane and peripheral arms
    • Sazanov L.A., Walker J.E. Cryo-electron crystallography of two sub-complexes of bovine complex I reveals the relationship between the membrane and peripheral arms. J. Mol. Biol 2000, 302(2):455-464.
    • (2000) J. Mol. Biol , vol.302 , Issue.2 , pp. 455-464
    • Sazanov, L.A.1    Walker, J.E.2
  • 271
    • 36048949714 scopus 로고    scopus 로고
    • Reconstitution of mitochondrial ATP synthase into lipid bilayers for structural analysis
    • Arechaga I., Fotiadis D. Reconstitution of mitochondrial ATP synthase into lipid bilayers for structural analysis. J. Struct. Biol. 2007, 160(3):287-294.
    • (2007) J. Struct. Biol. , vol.160 , Issue.3 , pp. 287-294
    • Arechaga, I.1    Fotiadis, D.2
  • 272
    • 31344435814 scopus 로고    scopus 로고
    • Two-dimensional crystallization and analysis of projection images of intact Thermus thermophilus V-ATPase
    • Gerle C., Tani K., Yokoyama K., Tamakoshi M., Yoshida M., Fujiyoshi Y., Mitsuoka K. Two-dimensional crystallization and analysis of projection images of intact Thermus thermophilus V-ATPase. J. Struct. Biol. 2006, 153(2):200-206.
    • (2006) J. Struct. Biol. , vol.153 , Issue.2 , pp. 200-206
    • Gerle, C.1    Tani, K.2    Yokoyama, K.3    Tamakoshi, M.4    Yoshida, M.5    Fujiyoshi, Y.6    Mitsuoka, K.7
  • 275
    • 33751091503 scopus 로고    scopus 로고
    • Structural investigations of the membrane-embedded rotor ring of the F-ATPase from Clostridium paradoxum
    • Meier T., Ferguson S.A., Cook G.M., Dimroth P., Vonck J. Structural investigations of the membrane-embedded rotor ring of the F-ATPase from Clostridium paradoxum. J. Bacteriol. 2006, 188(22):7759-7764.
    • (2006) J. Bacteriol. , vol.188 , Issue.22 , pp. 7759-7764
    • Meier, T.1    Ferguson, S.A.2    Cook, G.M.3    Dimroth, P.4    Vonck, J.5
  • 276
    • 42449164685 scopus 로고    scopus 로고
    • An intermediate step in the evolution of ATPases: A hybrid F(0)-V(0) rotor in a bacterial Na(+) F(1)F(0) ATP synthase
    • Fritz M., Klyszejko A.L., Morgner N., Vonck J., Brutschy B., Muller D.J., Meier T., Müller V. An intermediate step in the evolution of ATPases: A hybrid F(0)-V(0) rotor in a bacterial Na(+) F(1)F(0) ATP synthase. FEBS J. 2008, 275(9):1999-2007.
    • (2008) FEBS J. , vol.275 , Issue.9 , pp. 1999-2007
    • Fritz, M.1    Klyszejko, A.L.2    Morgner, N.3    Vonck, J.4    Brutschy, B.5    Muller, D.J.6    Meier, T.7    Müller, V.8
  • 277
    • 64649086247 scopus 로고    scopus 로고
    • The c13 ring from a thermoalkaliphilic ATP synthase reveals an extended diameter due to a special structural region
    • Matthies D., Preiss L., Klyszejko A.L., Müller D.J., Cook G.M., Vonck J., Meier T. The c13 ring from a thermoalkaliphilic ATP synthase reveals an extended diameter due to a special structural region. J. Mol. Biol. 2009, 388(3):611-618.
    • (2009) J. Mol. Biol. , vol.388 , Issue.3 , pp. 611-618
    • Matthies, D.1    Preiss, L.2    Klyszejko, A.L.3    Müller, D.J.4    Cook, G.M.5    Vonck, J.6    Meier, T.7
  • 279
    • 42449127446 scopus 로고    scopus 로고
    • Membrane structure of CtrA3, a copper-transporting P-type-ATPase from Aquifex aeolicus
    • Chintalapati S., Al Kurdi R., van Scheltinga A.C., Kühlbrandt W. Membrane structure of CtrA3, a copper-transporting P-type-ATPase from Aquifex aeolicus. J. Mol. Biol. 2008, 378(3):581-595.
    • (2008) J. Mol. Biol. , vol.378 , Issue.3 , pp. 581-595
    • Chintalapati, S.1    Al Kurdi, R.2    van Scheltinga, A.C.3    Kühlbrandt, W.4
  • 280
    • 44649182134 scopus 로고    scopus 로고
    • Structure of a copper pump suggests a regulatory role for its metal-binding domain
    • Wu C.C., Rice W.J., Stokes D.L. Structure of a copper pump suggests a regulatory role for its metal-binding domain. Structure 2008, 16(6):976-985.
    • (2008) Structure , vol.16 , Issue.6 , pp. 976-985
    • Wu, C.C.1    Rice, W.J.2    Stokes, D.L.3
  • 282
    • 67049131994 scopus 로고    scopus 로고
    • +-ATPase prevents reverse reaction of the transport cycle
    • +-ATPase prevents reverse reaction of the transport cycle. EMBO J. 2009, 28(11):1637-1643.
    • (2009) EMBO J. , vol.28 , Issue.11 , pp. 1637-1643
    • Abe, K.1    Tani, K.2    Nishizawa, T.3    Fujiyoshi, Y.4
  • 283
    • 0032545098 scopus 로고    scopus 로고
    • Three-dimensional crystals of Ca2+-ATPase from sarcoplasmic reticulum: Merging electron diffraction tilt series and imaging the (h, k, 0) projection
    • Shi D., Lewis M.R., Young H.S., Stokes D.L. Three-dimensional crystals of Ca2+-ATPase from sarcoplasmic reticulum: Merging electron diffraction tilt series and imaging the (h, k, 0) projection. J. Mol. Biol. 1998, 284(5):1547-1564.
    • (1998) J. Mol. Biol. , vol.284 , Issue.5 , pp. 1547-1564
    • Shi, D.1    Lewis, M.R.2    Young, H.S.3    Stokes, D.L.4
  • 284
    • 0032560170 scopus 로고    scopus 로고
    • Structure of the calcium pump from sarcoplasmic reticulum at 8 Å resolution
    • Zhang P., Toyoshima C., Yonekura K., Green N.M., Stokes D.L. Structure of the calcium pump from sarcoplasmic reticulum at 8 Å resolution. Nature 1998, 392(6678):835-839.
    • (1998) Nature , vol.392 , Issue.6678 , pp. 835-839
    • Zhang, P.1    Toyoshima, C.2    Yonekura, K.3    Green, N.M.4    Stokes, D.L.5
  • 285
    • 0036300446 scopus 로고    scopus 로고
    • A structural model for the catalytic cycle of Ca(2+)-ATPase
    • Xu C., Rice W.J., He W., Stokes D.L. A structural model for the catalytic cycle of Ca(2+)-ATPase. J. Mol. Biol. 2002, 316(1):201-211.
    • (2002) J. Mol. Biol. , vol.316 , Issue.1 , pp. 201-211
    • Xu, C.1    Rice, W.J.2    He, W.3    Stokes, D.L.4
  • 288
    • 0030926823 scopus 로고    scopus 로고
    • How to make tubular crystals by reconstitution of detergent-solubilized Ca2(+)-ATPase
    • Young H.S., Rigaud J.L., Lacapere J.J., Reddy L.G., Stokes D.L. How to make tubular crystals by reconstitution of detergent-solubilized Ca2(+)-ATPase. Biophys. J. 1997, 72(6):2545-2558.
    • (1997) Biophys. J. , vol.72 , Issue.6 , pp. 2545-2558
    • Young, H.S.1    Rigaud, J.L.2    Lacapere, J.J.3    Reddy, L.G.4    Stokes, D.L.5
  • 290
    • 0032772540 scopus 로고    scopus 로고
    • Reconstitution of detergent-solubilized Na,K-ATPase and formation of two-dimensional crystals
    • Mohraz M. Reconstitution of detergent-solubilized Na,K-ATPase and formation of two-dimensional crystals. J. Struct. Biol. 1999, 125(1):76-85.
    • (1999) J. Struct. Biol. , vol.125 , Issue.1 , pp. 76-85
    • Mohraz, M.1
  • 293
    • 40749146863 scopus 로고    scopus 로고
    • Three-dimensional structure of the KdpFABC complex of Escherichia coli by electron tomography of two-dimensional crystals
    • Hu G.B., Rice W.J., Drose S., Altendorf K., Stokes D.L. Three-dimensional structure of the KdpFABC complex of Escherichia coli by electron tomography of two-dimensional crystals. J. Struct. Biol. 2008, 161(3):411-418.
    • (2008) J. Struct. Biol. , vol.161 , Issue.3 , pp. 411-418
    • Hu, G.B.1    Rice, W.J.2    Drose, S.3    Altendorf, K.4    Stokes, D.L.5
  • 294
    • 0021111915 scopus 로고
    • Two-dimensional crystal packing of matrix porin. A channel forming protein in Escherichia coli outer membranes
    • Dorset D.L., Engel A., Haner M., Massalski A., Rosenbusch J.P. Two-dimensional crystal packing of matrix porin. A channel forming protein in Escherichia coli outer membranes. J. Mol. Biol. 1983, 165(4):701-710.
    • (1983) J. Mol. Biol. , vol.165 , Issue.4 , pp. 701-710
    • Dorset, D.L.1    Engel, A.2    Haner, M.3    Massalski, A.4    Rosenbusch, J.P.5
  • 297
    • 0033563307 scopus 로고    scopus 로고
    • An 8-A projected structure of FhuA, A "ligand-gated" channel of the Escherichia coli outer membrane
    • Lambert O., Moeck G.S., Levy D., Plancon L., Letellier L., Rigaud J.L. An 8-A projected structure of FhuA, A "ligand-gated" channel of the Escherichia coli outer membrane. J. Struct. Biol. 1999, 126(2):145-155.
    • (1999) J. Struct. Biol. , vol.126 , Issue.2 , pp. 145-155
    • Lambert, O.1    Moeck, G.S.2    Levy, D.3    Plancon, L.4    Letellier, L.5    Rigaud, J.L.6
  • 298
    • 0023744872 scopus 로고
    • Three-dimensional reconstruction of maltoporin from electron microscopy and image processing
    • Lepault J., Dargent B., Tichelaar W., Rosenbusch J.P., Leonard K., Pattus F. Three-dimensional reconstruction of maltoporin from electron microscopy and image processing. EMBO J. 1988, 7(1):261-268.
    • (1988) EMBO J. , vol.7 , Issue.1 , pp. 261-268
    • Lepault, J.1    Dargent, B.2    Tichelaar, W.3    Rosenbusch, J.P.4    Leonard, K.5    Pattus, F.6
  • 300
    • 0035808445 scopus 로고    scopus 로고
    • Projection structure of the monomeric porin OmpG at 6 A resolution
    • Behlau M., Mills D.J., Quader H., Kühlbrandt W., Vonck J. Projection structure of the monomeric porin OmpG at 6 A resolution. J. Mol. Biol. 2001, 305(1):71-77.
    • (2001) J. Mol. Biol. , vol.305 , Issue.1 , pp. 71-77
    • Behlau, M.1    Mills, D.J.2    Quader, H.3    Kühlbrandt, W.4    Vonck, J.5
  • 301
    • 0033784649 scopus 로고    scopus 로고
    • Expression, two-dimensional crystallization, and three-dimensional reconstruction of the beta8 outer membrane protein Omp21 from Comamonas acidovorans
    • Baldermann C., Engelhardt H. Expression, two-dimensional crystallization, and three-dimensional reconstruction of the beta8 outer membrane protein Omp21 from Comamonas acidovorans. J. Struct. Biol. 2000, 131(2):96-107.
    • (2000) J. Struct. Biol. , vol.131 , Issue.2 , pp. 96-107
    • Baldermann, C.1    Engelhardt, H.2
  • 302
    • 0032934816 scopus 로고    scopus 로고
    • Derrick, J. Projection structure of reconstituted Opc outer membrane protein from Neisseria meningitidis
    • Collins R., Achtman M., Ford R., Bullough P. Derrick, J. Projection structure of reconstituted Opc outer membrane protein from Neisseria meningitidis. Mol. Microbiol. 1999, 32(1):217-219.
    • (1999) Mol. Microbiol. , vol.32 , Issue.1 , pp. 217-219
    • Collins, R.1    Achtman, M.2    Ford, R.3    Bullough, P.4
  • 303
    • 0024278074 scopus 로고
    • High-resolution electron diffraction of reconstituted PhoE porin
    • Jap B.K. High-resolution electron diffraction of reconstituted PhoE porin. J. Mol. Biol. 1988, 199(1):229-231.
    • (1988) J. Mol. Biol. , vol.199 , Issue.1 , pp. 229-231
    • Jap, B.K.1
  • 305
    • 0021139243 scopus 로고
    • Two configurations of a channel-forming membrane protein
    • Unwin P.N., Ennis P.D. Two configurations of a channel-forming membrane protein. Nature 1984, 307(5952):609-613.
    • (1984) Nature , vol.307 , Issue.5952 , pp. 609-613
    • Unwin, P.N.1    Ennis, P.D.2
  • 306
    • 0031012580 scopus 로고    scopus 로고
    • Three-dimensional structure of the gap junction connexon
    • 2 PT 1
    • Perkins G., Goodenough D., Sosinsky G. Three-dimensional structure of the gap junction connexon. Biophys. J. 1997, 72(2 Pt 1):533-544.
    • (1997) Biophys. J. , vol.72 , pp. 533-544
    • Perkins, G.1    Goodenough, D.2    Sosinsky, G.3
  • 307
    • 0033386437 scopus 로고    scopus 로고
    • Expression, two-dimensional crystallization, and electron cryo-crystallography of recombinant gap junction membrane channels
    • Unger V.M., Kumar N.M., Gilula N.B., Yeager M. Expression, two-dimensional crystallization, and electron cryo-crystallography of recombinant gap junction membrane channels. J. Struct. Biol. 1999, 128(1):98-105.
    • (1999) J. Struct. Biol. , vol.128 , Issue.1 , pp. 98-105
    • Unger, V.M.1    Kumar, N.M.2    Gilula, N.B.3    Yeager, M.4
  • 308
    • 0033582686 scopus 로고    scopus 로고
    • Three-dimensional structure of a recombinant gap junction membrane channel
    • Unger V.M., Kumar N.M., Gilula N.B., Yeager M. Three-dimensional structure of a recombinant gap junction membrane channel. Science 1999, 283(5405):1176-1180.
    • (1999) Science , vol.283 , Issue.5405 , pp. 1176-1180
    • Unger, V.M.1    Kumar, N.M.2    Gilula, N.B.3    Yeager, M.4
  • 309
    • 0347756747 scopus 로고    scopus 로고
    • Projection structure of full length connexin 43 by electron cryo-crystallography
    • Cheng A., Schweissinger D., Dawood F., Kumar N., Yeager M. Projection structure of full length connexin 43 by electron cryo-crystallography. Cell Commun. Adhes. 2003, 10(4-6):187-191.
    • (2003) Cell Commun. Adhes. , vol.10 , Issue.4-6 , pp. 187-191
    • Cheng, A.1    Schweissinger, D.2    Dawood, F.3    Kumar, N.4    Yeager, M.5
  • 310
    • 34547224262 scopus 로고    scopus 로고
    • Three-dimensional structure of a human connexin26 gap junction channel reveals a plug in the vestibule
    • Oshima A., Tani K., Hiroaki Y., Fujiyoshi Y., Sosinsky G.E. Three-dimensional structure of a human connexin26 gap junction channel reveals a plug in the vestibule. Proc. Natl. Acad. Sci. USA 2007, 104(24):10034-10039.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.24 , pp. 10034-10039
    • Oshima, A.1    Tani, K.2    Hiroaki, Y.3    Fujiyoshi, Y.4    Sosinsky, G.E.5
  • 312
    • 0031787554 scopus 로고    scopus 로고
    • Three-dimensional structure of membrane proteins determined by two-dimensional crystallization, electron cryomicroscopy, and image analysis
    • Yeager M., Unger V.M., Mitra A.K. Three-dimensional structure of membrane proteins determined by two-dimensional crystallization, electron cryomicroscopy, and image analysis. Meth. Enzymol 1999, 294:135-180.
    • (1999) Meth. Enzymol , vol.294 , pp. 135-180
    • Yeager, M.1    Unger, V.M.2    Mitra, A.K.3
  • 313
    • 48449105610 scopus 로고    scopus 로고
    • Projection structure of a N-terminal deletion mutant of connexin 26 channel with decreased central pore density
    • Oshima A., Tani K., Hiroaki Y., Fujiyoshi Y., Sosinsky G.E. Projection structure of a N-terminal deletion mutant of connexin 26 channel with decreased central pore density. Cell Commun. Adhes. 2008, 15(1):85-93.
    • (2008) Cell Commun. Adhes. , vol.15 , Issue.1 , pp. 85-93
    • Oshima, A.1    Tani, K.2    Hiroaki, Y.3    Fujiyoshi, Y.4    Sosinsky, G.E.5
  • 314
    • 0035940960 scopus 로고    scopus 로고
    • Structure of the major membrane protein complex from urinary bladder epithelial cells by cryo-electron crystallography
    • Oostergetel G.T., Keegstra W., Brisson A. Structure of the major membrane protein complex from urinary bladder epithelial cells by cryo-electron crystallography. J. Mol. Biol 2001, 314(2):245-252.
    • (2001) J. Mol. Biol , vol.314 , Issue.2 , pp. 245-252
    • Oostergetel, G.T.1    Keegstra, W.2    Brisson, A.3
  • 315
    • 34547899224 scopus 로고    scopus 로고
    • Two conformational states of the membrane-associated Bacillus thuringiensis Cry4Ba delta-endotoxin complex revealed by electron crystallography: Implications for toxin-pore formation
    • Ounjai P., Unger V.M., Sigworth F.J., Angsuthanasombat C. Two conformational states of the membrane-associated Bacillus thuringiensis Cry4Ba delta-endotoxin complex revealed by electron crystallography: Implications for toxin-pore formation. Biochem. Biophys. Res. Commun. 2007, 361(4):890-895.
    • (2007) Biochem. Biophys. Res. Commun. , vol.361 , Issue.4 , pp. 890-895
    • Ounjai, P.1    Unger, V.M.2    Sigworth, F.J.3    Angsuthanasombat, C.4
  • 316
    • 0343091467 scopus 로고    scopus 로고
    • Two-dimensional crystallization on lipid monolayers and three-dimensional structure of sticholysin II, a cytolysin from the sea anemone Stichodactyla helianthus
    • Martin-Benito J., Gavilanes F., de Los Rios V., Mancheno J.M., Fernandez J.J., Gavilanes J.G. Two-dimensional crystallization on lipid monolayers and three-dimensional structure of sticholysin II, a cytolysin from the sea anemone Stichodactyla helianthus. Biophys. J. 2000, 78(6):3186-3194.
    • (2000) Biophys. J. , vol.78 , Issue.6 , pp. 3186-3194
    • Martin-Benito, J.1    Gavilanes, F.2    de Los Rios, V.3    Mancheno, J.M.4    Fernandez, J.J.5    Gavilanes, J.G.6
  • 317
    • 0242542032 scopus 로고    scopus 로고
    • Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation
    • Mancheno J.M., Martin-Benito J., Martinez-Ripoll M., Gavilanes J.G., Hermoso J.A. Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation. Structure 2003, 11(11):1319-1328.
    • (2003) Structure , vol.11 , Issue.11 , pp. 1319-1328
    • Mancheno, J.M.1    Martin-Benito, J.2    Martinez-Ripoll, M.3    Gavilanes, J.G.4    Hermoso, J.A.5
  • 318
    • 0026721371 scopus 로고
    • The aerolysin membrane channel is formed by heptamerization of the monomer
    • Wilmsen H.U., Leonard K.R., Tichelaar W., Buckley J.T., Pattus F. The aerolysin membrane channel is formed by heptamerization of the monomer. EMBO J. 1992, 11(7):2457-2463.
    • (1992) EMBO J. , vol.11 , Issue.7 , pp. 2457-2463
    • Wilmsen, H.U.1    Leonard, K.R.2    Tichelaar, W.3    Buckley, J.T.4    Pattus, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.