메뉴 건너뛰기




Volumn , Issue SUPPL.72, 2013, Pages

Overview of electron crystallography of membrane proteins: Crystallization and screening strategies using negative stain electron microscopy

Author keywords

Electron crystallography; Membrane proteins; Negative stain electron microscopy; Protein purification; Protein solubilization

Indexed keywords

ADENOSINE A2A RECEPTOR; DETERGENT; MEMBRANE PROTEIN; NEUROTENSIN RECEPTOR;

EID: 84879775726     PISSN: 19343655     EISSN: 19343663     Source Type: Journal    
DOI: 10.1002/0471140864.ps1715s72     Document Type: Article
Times cited : (20)

References (29)
  • 2
    • 0017807903 scopus 로고
    • Structure and orientation of cytochrome c oxidase in crystalline membranes
    • Frey, T.G., Chan, S.H.P., and Schatz, G. 1978. Structure and orientation of cytochrome c oxidase in crystalline membranes. J. Biol. Chem. 253:4389-4395.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4389-4395
    • Frey, T.G.1    Chan, S.H.P.2    Schatz, G.3
  • 3
    • 0031700068 scopus 로고    scopus 로고
    • The structural study of membrane proteins by electron crystallography
    • Fujiyoshi, Y. 1998. The structural study of membrane proteins by electron crystallography. Adv. Biophys. 35:25-80.
    • (1998) Adv. Biophys. , vol.35 , pp. 25-80
    • Fujiyoshi, Y.1
  • 4
    • 0033986513 scopus 로고    scopus 로고
    • Galectin-3 is associated with the plasma membrane of lens fiber cells
    • Gonen, T., Donaldson, P., and Kistler, J. 2000. Galectin-3 is associated with the plasma membrane of lens fiber cells. Invest. Ophthalmol. Vis. Sci. 41:199-203.
    • (2000) Invest. Ophthalmol. Vis. Sci. , vol.41 , pp. 199-203
    • Gonen, T.1    Donaldson, P.2    Kistler, J.3
  • 5
    • 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., andWalz, T. 2004. Aquaporin-0 membrane junctions reveal the structure of a closed water pore. Nature 429:193-197.
    • (2004) Nature , vol.429 , pp. 193-197
    • Gonen, T.1    Sliz, P.2    Kistler, J.3    Cheng, Y.4    Walz, T.5
  • 6
  • 7
    • 0023920896 scopus 로고
    • Large-scale chromatography of recombinant proteins
    • Hochuli, E. 1988. Large-scale chromatography of recombinant proteins. J. Chromatogr. 444:293-302.
    • (1988) J. Chromatogr. , vol.444 , pp. 293-302
    • Hochuli, E.1
  • 8
    • 0034707086 scopus 로고    scopus 로고
    • Interaction ofmembrane proteins and lipidswith solubilizing detergents
    • le Maire, M., Champeil, P., and Moller, J.V. 2000. Interaction ofmembrane proteins and lipidswith solubilizing detergents. Biochim. Biophys. Acta 1508:86-111.
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 86-111
    • le Maire, M.1    Champeil, P.2    Moller, J.V.3
  • 9
    • 37349111755 scopus 로고    scopus 로고
    • Projection structure of yidC: A conserved mediator of membrane protein assembly
    • Lotz, M., Haase, W.,Kuhlbrandt, W., andCollinson, I. 2008. Projection structure of yidC: A conserved mediator of membrane protein assembly. J. Mol. Biol. 375:901-907.
    • (2008) J. Mol. Biol. , vol.375 , pp. 901-907
    • Lotz, M.1    Haase, W.2    Kuhlbrandt, W.3    Collinson, I.4
  • 11
    • 36148942092 scopus 로고    scopus 로고
    • Breaking the bottleneck: Eukaryotic membrane protein expression for high-resolution structural studies
    • Midgett, C.R. and Madden, D.R. 2007. Breaking the bottleneck: Eukaryotic membrane protein expression for high-resolution structural studies. J. Struct. Biol. 160:265-274.
    • (2007) J. Struct. Biol. , vol.160 , pp. 265-274
    • Midgett, C.R.1    Madden, D.R.2
  • 12
    • 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. andWalker, J.E. 1996. 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. 260:289-298.
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 14
    • 79960678169 scopus 로고    scopus 로고
    • Reprogramming chaperone pathways to improve membrane protein expression in Escherichia coli
    • Nannenga, B.L. and Baneyx, F. 2011. Reprogramming chaperone pathways to improve membrane protein expression in Escherichia coli. Protein Sci. 20:1411-1420.
    • (2011) Protein Sci , vol.20 , pp. 1411-1420
    • Nannenga, B.L.1    Baneyx, F.2
  • 15
    • 79957809202 scopus 로고    scopus 로고
    • Advances in the production of membrane proteins in Pichia pastoris
    • Ramon, A. and Marin, M. 2011. Advances in the production of membrane proteins in Pichia pastoris. Biotechnol. J. 6:700-706.
    • (2011) Biotechnol. J. , vol.6 , pp. 700-706
    • Ramon, A.1    Marin, M.2
  • 16
    • 70349863382 scopus 로고    scopus 로고
    • Lipid-protein interactions probed by electron crystallography
    • Reichow, S.L. and Gonen, T. 2009. Lipid-protein interactions probed by electron crystallography. Curr. Opin. Struct. Biol. 19:560-565.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 560-565
    • Reichow, S.L.1    Gonen, T.2
  • 17
    • 0242573084 scopus 로고    scopus 로고
    • Membrane protein reconstitution and crystallization by controlled dilution
    • Ŕemigy, H.W., Caujolle-Bert, D. Suda, K., Schenk, A., Chami, M., and Engel, A. 2003. Membrane protein reconstitution and crystallization by controlled dilution. FEBS Lett. 555:160-169.
    • (2003) FEBS Lett , vol.555 , pp. 160-169
    • Ŕemigy, H.W.1    Caujolle-Bert, D.2    Suda, K.3    Schenk, A.4    Chami, M.5    Engel, A.6
  • 18
    • 0030949437 scopus 로고    scopus 로고
    • Bio-Beads: An efficient strategy for two-dimensional crystallization of membrane proteins
    • Rigaud, J.L., Mosser, G., Lacaperre, J.J., Olofsson, A., Levy, D., and Ranck, J.L. 1997. Bio-Beads: An efficient strategy for two-dimensional crystallization of membrane proteins. J. Struct. Biol. 118:226-235.
    • (1997) J. Struct. Biol. , vol.118 , pp. 226-235
    • Rigaud, J.L.1    Mosser, G.2    Lacaperre, J.J.3    Olofsson, A.4    Levy, D.5    Ranck, J.L.6
  • 19
    • 67650082450 scopus 로고    scopus 로고
    • Integrity of N- and C-termini is important for E. coli Hsp31 chaperone activity
    • Sastry, M.S., Zhou, W., and Baneyx, F. 2009. Integrity of N- and C-termini is important for E. coli Hsp31 chaperone activity. Protein Sci. 18:1439-1447.
    • (2009) Protein Sci , vol.18 , pp. 1439-1447
    • Sastry, M.S.1    Zhou, W.2    Baneyx, F.3
  • 20
    • 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. andWalker, J.E. 2000. Cryo-electron crystallography of two sub-complexes of bovine complex I reveals the relationship between the membrane and peripheral arms. J. Mol. Biol. 302:455-464.
    • (2000) J. Mol. Biol. , vol.302 , pp. 455-464
    • Sazanov, L.A.1    Walker, J.E.2
  • 21
    • 33846219153 scopus 로고    scopus 로고
    • Controlled 2D crystallization of membrane proteins using methyl-beta-cyclodextrin
    • Signorell, G.A., Kaufmann, T.C., Kukulski, W., Engel, A., and Remigy, H.W. 2007. Controlled 2D crystallization of membrane proteins using methyl-beta-cyclodextrin. J. Struct. Biol. 157:321-328.
    • (2007) J. Struct. Biol. , vol.157 , pp. 321-328
    • Signorell, G.A.1    Kaufmann, T.C.2    Kukulski, W.3    Engel, A.4    Remigy, H.W.5
  • 22
    • 33748129976 scopus 로고    scopus 로고
    • Comparative analysis and "expression space" coverage of the production of prokaryotic membrane proteins for structural genomics
    • Surade, S., Klein, M., Stolt-Bergner, P.C., Muenke, C., Roy, A., and Michel, H. 2006. Comparative analysis and "expression space" coverage of the production of prokaryotic membrane proteins for structural genomics. Protein Sci. 15:2178-2189.
    • (2006) Protein Sci , vol.15 , pp. 2178-2189
    • Surade, S.1    Klein, M.2    Stolt-Bergner, P.C.3    Muenke, C.4    Roy, A.5    Michel, H.6
  • 23
    • 0029838532 scopus 로고    scopus 로고
    • Purification of a rat neurotensin receptor expressed in Escherichia coli
    • Tucker, J. and Grisshammer, R. 1996. Purification of a rat neurotensin receptor expressed in Escherichia coli. Biochem. J. 317:891-899.
    • (1996) Biochem. J. , vol.317 , pp. 891-899
    • Tucker, J.1    Grisshammer, R.2
  • 24
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4A resolution
    • Unwin, N. 2005. Refined structure of the nicotinic acetylcholine receptor at 4A resolution. J. Mol. Biol. 346:967-989.
    • (2005) J. Mol. Biol. , vol.346 , pp. 967-989
    • Unwin, N.1
  • 25
    • 33847063568 scopus 로고    scopus 로고
    • Projection map of aquaporin-9 at 7 A resolution
    • Viadiu, H., Gonen, T., andWalz, T. 2007. Projection map of aquaporin-9 at 7 A resolution. J. Mol. Biol. 367:80-88.
    • (2007) J. Mol. Biol. , vol.367 , pp. 80-88
    • Viadiu, H.1    Gonen, T.2    Walz, T.3
  • 27
    • 12244292640 scopus 로고    scopus 로고
    • Purification and characterization of the human adenosine A(2a) receptor functionally expressed in Escherichia coli
    • Weiss, H.M. and Grisshammer, R. 2002. Purification and characterization of the human adenosine A(2a) receptor functionally expressed in Escherichia coli. Eur. J. Biochem. 269:82-92.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 82-92
    • Weiss, H.M.1    Grisshammer, R.2
  • 28
    • 0033168715 scopus 로고    scopus 로고
    • Projection structure of NhaA, a secondary transporter from Escherichia coli, at4.0Aresolution
    • Williams, K.A., Geldmacher-Kaufer, U., Padan, E., Schuldiner, S., and Kuhlbrandt, W. 1999. Projection structure of NhaA, a secondary transporter from Escherichia coli, at 4.0Aresolution. EMBO J. 18:3558-3563.
    • (1999) EMBO J , vol.18 , pp. 3558-3563
    • Williams, K.A.1    Geldmacher-Kaufer, U.2    Padan, E.3    Schuldiner, S.4    Kuhlbrandt, W.5
  • 29
    • 80054063377 scopus 로고    scopus 로고
    • Advances in structural and functional analysis of membrane proteins by electron crystallography
    • Wisedchaisri, G., Reichow, S.L., and Gonen, T. 2011. Advances in structural and functional analysis of membrane proteins by electron crystallography. Structure 19:1381-1393.
    • (2011) Structure , vol.19 , pp. 1381-1393
    • Wisedchaisri, G.1    Reichow, S.L.2    Gonen, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.