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Volumn 19, Issue 7, 2011, Pages 976-987

Fragment-based phase extension for three-dimensional structure determination of membrane proteins by electron crystallography

Author keywords

[No Author keywords available]

Indexed keywords

AQUAPORIN 0; AQUAPORIN 4; BACTERIORHODOPSIN; LIGAND; LIPID; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 79960194104     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2011.04.008     Document Type: Article
Times cited : (19)

References (44)
  • 2
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4) The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 6
    • 0031700068 scopus 로고    scopus 로고
    • The structural study of membrane proteins by electron crystallography
    • DOI 10.1016/S0065-227X(98)80003-8
    • Y. Fujiyoshi The structural study of membrane proteins by electron crystallography Adv. Biophys. 35 1998 25 80 (Pubitemid 28566345)
    • (1998) Advances in Biophysics , vol.35 , pp. 25-80
    • Fujiyoshi, Y.1
  • 7
    • 0027724446 scopus 로고
    • High-resolution electron crystallography of protein molecules
    • DOI 10.1016/0304-3991(93)90064-5
    • R.M. Glaeser, and K.H. Downing High-resolution electron crystallography of protein molecules Ultramicroscopy 52 1993 478 486 (Pubitemid 24051255)
    • (1993) Ultramicroscopy , vol.52 , Issue.3-4 , pp. 478-486
    • Glaeser, R.M.1    Downing, K.H.2
  • 8
    • 33845669996 scopus 로고    scopus 로고
    • The structure of aquaporins
    • DOI 10.1017/S0033583506004458, PII S0033583506004458
    • T. Gonen, and T. Walz The structure of aquaporins Q. Rev. Biophys. 39 2006 361 396 (Pubitemid 44950380)
    • (2006) Quarterly Reviews of Biophysics , vol.39 , Issue.4 , pp. 361-396
    • Gonen, T.1    Walz, T.2
  • 9
    • 2442659197 scopus 로고    scopus 로고
    • Aquaporin-0 membrane junctions reveal the structure of a closed water pore
    • DOI 10.1038/nature02503
    • T. Gonen, P. Sliz, J. Kistler, Y. Cheng, and T. Walz Aquaporin-0 membrane junctions reveal the structure of a closed water pore Nature 429 2004 193 197 (Pubitemid 38656196)
    • (2004) Nature , vol.429 , Issue.6988 , pp. 193-197
    • Gonen, T.1    Silz, P.2    Kistler, J.3    Cheng, Y.4    Walz, T.5
  • 10
    • 28444450878 scopus 로고    scopus 로고
    • Lipid-protein interactions in double-layered two-dimensional AQP0 crystals
    • DOI 10.1038/nature04321
    • T. Gonen, Y. Cheng, P. Sliz, Y. Hiroaki, Y. Fujiyoshi, S.C. Harrison, and T. Walz Lipid-protein interactions in double-layered two-dimensional AQP0 crystals Nature 438 2005 633 638 (Pubitemid 41740568)
    • (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
  • 12
    • 1942521362 scopus 로고    scopus 로고
    • Improved specimen preparation for cryo-electron microscopy using a symmetric carbon sandwich technique
    • DOI 10.1016/j.jsb.2004.01.012, PII S1047847704000310
    • N. Gyobu, K. Tani, Y. Hiroaki, A. Kamegawa, K. Mitsuoka, and Y. Fujiyoshi Improved specimen preparation for cryo-electron microscopy using a symmetric carbon sandwich technique J. Struct. Biol. 146 2004 325 333 (Pubitemid 38507434)
    • (2004) Journal of Structural Biology , 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
  • 14
    • 0000980729 scopus 로고
    • Representation of phase probability distributions for simplified combination of independent phase information
    • W.A. Hendrickson, and E.E. Lattman Representation of phase probability distributions for simplified combination of independent phase information Acta Crystallogr. B 26 1970 136 143
    • (1970) Acta Crystallogr. B , vol.26 , pp. 136-143
    • Hendrickson, W.A.1    Lattman, E.E.2
  • 16
    • 77952584138 scopus 로고    scopus 로고
    • Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals
    • R.K. Hite, Z. Li, and T. Walz Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals EMBO J. 29 2010 1652 1658
    • (2010) EMBO J. , vol.29 , pp. 1652-1658
    • Hite, R.K.1    Li, Z.2    Walz, T.3
  • 17
    • 0022409872 scopus 로고
    • Three-dimensional structure of poliovirus at 2.9 A resolution
    • J.M. Hogle, M. Chow, and D.J. Filman Three-dimensional structure of poliovirus at 2.9 A resolution Science 229 1985 1358 1365 (Pubitemid 16222374)
    • (1985) Science , vol.229 , Issue.4720 , pp. 1358-1365
    • Hogle, J.M.1    Chow, M.2    Filman, D.J.3
  • 18
    • 0022192011 scopus 로고
    • Effects of the alpha-helix dipole upon the functioning and structure of proteins and peptides
    • W.G. Hol Effects of the alpha-helix dipole upon the functioning and structure of proteins and peptides Adv. Biophys. 19 1985 133 165
    • (1985) Adv. Biophys. , vol.19 , pp. 133-165
    • Hol, W.G.1
  • 19
    • 0017881332 scopus 로고
    • The alpha-helix dipole and the properties of proteins
    • W.G. Hol, P.T. van Duijnen, and H.J. Berendsen The alpha-helix dipole and the properties of proteins Nature 273 1978 443 446
    • (1978) Nature , vol.273 , pp. 443-446
    • Hol, W.G.1    Van Duijnen, P.T.2    Berendsen, H.J.3
  • 22
    • 68249144241 scopus 로고    scopus 로고
    • Similar energetic contributions of packing in the core of membrane and water-soluble proteins
    • N.H. Joh, A. Oberai, D. Yang, J.P. Whitelegge, and J.U. Bowie Similar energetic contributions of packing in the core of membrane and water-soluble proteins J. Am. Chem. Soc. 131 2009 10846 10847
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 10846-10847
    • Joh, N.H.1    Oberai, A.2    Yang, D.3    Whitelegge, J.P.4    Bowie, J.U.5
  • 24
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • DOI 10.1107/S0907444904026460
    • E. Krissinel, and K. Henrick Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallogr. D Biol. Crystallogr. 60 2004 2256 2268 (Pubitemid 41742778)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.12 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 25
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • DOI 10.1038/367614a0
    • W. Kuhlbrandt, D.N. Wang, and Y. Fujiyoshi Atomic model of plant light-harvesting complex by electron crystallography Nature 367 1994 614 621 (Pubitemid 24067701)
    • (1994) Nature , vol.367 , Issue.6464 , pp. 614-621
    • Kuhlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 26
    • 0034712851 scopus 로고    scopus 로고
    • The three-dimensional structure of halorhodopsin to 5 A by electron crystallography: A new unbending procedure for two-dimensional crystals by using a global reference structure
    • DOI 10.1073/pnas.080064697
    • E.R. Kunji, S. von Gronau, D. Oesterhelt, and R. Henderson The three-dimensional structure of halorhodopsin to 5 A by electron crystallography: A new unbending procedure for two-dimensional crystals by using a global reference structure Proc. Natl. Acad. Sci. USA 97 2000 4637 4642 (Pubitemid 30238610)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.9 , pp. 4637-4642
    • Kunji, E.R.S.1    Von Gronau, S.2    Oesterhelt, D.3    Henderson, R.4
  • 29
    • 0033605231 scopus 로고    scopus 로고
    • The structure of bacteriorhodopsin at 3.0 A resolution based on electron crystallography: Implication of the charge distribution
    • DOI 10.1006/jmbi.1998.2529
    • K. Mitsuoka, T. Hirai, K. Murata, A. Miyazawa, A. Kidera, Y. Kimura, and Y. Fujiyoshi The structure of bacteriorhodopsin at 3.0 A resolution based on electron crystallography: implication of the charge distribution J. Mol. Biol. 286 1999 861 882 (Pubitemid 29106223)
    • (1999) Journal of Molecular Biology , 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
  • 33
    • 0033536662 scopus 로고    scopus 로고
    • X-ray crystallographic structure of the Norwalk virus capsid
    • DOI 10.1126/science.286.5438.287
    • B.V. Prasad, M.E. Hardy, T. Dokland, J. Bella, M.G. Rossmann, and M.K. Estes X-ray crystallographic structure of the Norwalk virus capsid Science 286 1999 287 290 (Pubitemid 29484691)
    • (1999) Science , vol.286 , Issue.5438 , pp. 287-290
    • Prasad, B.V.V.1    Hardy, M.E.2    Dokland, T.3    Bella, J.4    Rossmann, M.G.5    Estes, M.K.6
  • 34
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • R.J. Read Improved Fourier coefficients for maps using phases from partial structures with errors Acta Crystallogr. A 42 1986 140 149
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 35
    • 70349863382 scopus 로고    scopus 로고
    • Lipid-protein interactions probed by electron crystallography
    • S.L. Reichow, and T. Gonen Lipid-protein interactions probed by electron crystallography Curr. Opin. Struct. Biol. 19 2009 560 565
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 560-565
    • Reichow, S.L.1    Gonen, T.2
  • 37
    • 0142167711 scopus 로고
    • Refinement of structures partially determined by isomorphous replacement method
    • M.G. Rossmann, and D.M. Blow Refinement of structures partially determined by isomorphous replacement method Acta Crystallogr. 14 1961 641 647
    • (1961) Acta Crystallogr. , vol.14 , pp. 641-647
    • Rossmann, M.G.1    Blow, D.M.2
  • 38
    • 0022401514 scopus 로고
    • Structure of a human common cold virus and functional relationship to other picornaviruses
    • DOI 10.1038/317145a0
    • M.G. Rossmann, E. Arnold, J.W. Erickson, E.A. Frankenberger, J.P. Griffith, H.J. Hecht, J.E. Johnson, G. Kamer, M. Luo, and A.G. Mosser Structure of a human common cold virus and functional relationship to other picornaviruses Nature 317 1985 145 153 (Pubitemid 16243130)
    • (1985) Nature , vol.317 , Issue.6033 , pp. 145-153
    • Rossmann, M.G.1    Arnold, E.2    Erickson, J.W.3
  • 39
    • 0034632864 scopus 로고    scopus 로고
    • Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
    • DOI 10.1038/35020614
    • S. Subramaniam, and R. Henderson Molecular mechanism of vectorial proton translocation by bacteriorhodopsin Nature 406 2000 653 657 (Pubitemid 30641055)
    • (2000) Nature , vol.406 , Issue.6796 , pp. 653-657
    • Subramanlam, S.1    Henderson, R.2
  • 42
    • 0038793604 scopus 로고    scopus 로고
    • Improving macromolecular atomic models at moderate resolution by automated iterative model building, statistical density modification and refinement
    • DOI 10.1107/S0907444903009922
    • T.C. Terwilliger Improving macromolecular atomic models at moderate resolution by automated iterative model building, statistical density modification and refinement Acta Crystallogr. D Biol. Crystallogr. 59 2003 1174 1182 (Pubitemid 36872353)
    • (2003) Acta Crystallographica Section D: Biological Crystallography , vol.59 , Issue.7 , pp. 1174-1182
    • Terwilliger, T.C.1
  • 43
    • 0035788131 scopus 로고    scopus 로고
    • Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps
    • DOI 10.1107/S0907444901012409
    • A.A. Vagin, and M.N. Isupov Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps Acta Crystallogr. D Biol. Crystallogr. 57 2001 1451 1456 (Pubitemid 36117196)
    • (2001) Acta Crystallographica Section D: Biological Crystallography , vol.57 , Issue.10 , pp. 1451-1456
    • Vagin, A.A.1    Isupov, M.N.2
  • 44
    • 0034658269 scopus 로고    scopus 로고
    • Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography
    • J. Vonck Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography EMBO J. 19 2000 2152 2160 (Pubitemid 30258996)
    • (2000) EMBO Journal , vol.19 , Issue.10 , pp. 2152-2160
    • Vonck, J.1


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