메뉴 건너뛰기




Volumn 13, Issue 3, 2005, Pages 363-372

Electron cryomicroscopy of biological machines at subnanometer resolution

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; F ACTIN; PROTEIN SUBUNIT; VIRUS PROTEIN;

EID: 14844325731     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2004.12.016     Document Type: Review
Times cited : (121)

References (48)
  • 1
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: Preparing the next generation of molecular biologists
    • B. Alberts The cell as a collection of protein machines: preparing the next generation of molecular biologists Cell 92 1998 291 294
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 2
    • 0026501223 scopus 로고
    • Unscrambling the puzzle of biological machines: The importance of the details
    • B. Alberts, and R. Miake-Lye Unscrambling the puzzle of biological machines: the importance of the details Cell 68 1992 415 420
    • (1992) Cell , vol.68 , pp. 415-420
    • Alberts, B.1    Miake-Lye, R.2
  • 3
    • 0041347832 scopus 로고    scopus 로고
    • Architecture of the herpes simplex virus major capsid protein derived from structural bioinformatics
    • M.L. Baker, W. Jiang, B.R. Bowman, Z.H. Zhou, F.A. Quiocho, F.J. Rixon, and W. Chiu Architecture of the herpes simplex virus major capsid protein derived from structural bioinformatics J. Mol. Biol. 331 2003 447 456
    • (2003) J. Mol. Biol. , vol.331 , pp. 447-456
    • Baker, M.L.1    Jiang, W.2    Bowman, B.R.3    Zhou, Z.H.4    Quiocho, F.A.5    Rixon, F.J.6    Chiu, W.7
  • 4
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • N. Ban, P. Nissen, J. Hansen, P.B. Moore, and T.A. Steitz The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution Science 289 2000 905 920
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 5
    • 1242351230 scopus 로고    scopus 로고
    • Experimental verification of conformational variation of human fatty acid synthase as predicted by normal mode analysis
    • J. Brink, S.J. Ludtke, Y. Kong, S.J. Wakil, J. Ma, and W. Chiu Experimental verification of conformational variation of human fatty acid synthase as predicted by normal mode analysis Structure 12 2004 185 191
    • (2004) Structure , vol.12 , pp. 185-191
    • Brink, J.1    Ludtke, S.J.2    Kong, Y.3    Wakil, S.J.4    Ma, J.5    Chiu, W.6
  • 6
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • D. Caspar, and A. Klug Physical principles in the construction of regular viruses Cold Spring Harb. Symp. Quant. Biol. 27 1962 1 24
    • (1962) Cold Spring Harb. Symp. Quant. Biol. , vol.27 , pp. 1-24
    • Caspar, D.1    Klug, A.2
  • 8
    • 10344227184 scopus 로고    scopus 로고
    • Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating
    • A. Fotin, Y. Cheng, N. Grigorieff, T. Walz, S.C. Harrison, and T. Kirchhausen Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating Nature 432 2004 649 653
    • (2004) Nature , vol.432 , pp. 649-653
    • Fotin, A.1    Cheng, Y.2    Grigorieff, N.3    Walz, T.4    Harrison, S.C.5    Kirchhausen, T.6
  • 12
    • 0015106320 scopus 로고
    • Limitations to significant information in biological electron microscopy as a result of radiation damage
    • R.M. Glaeser Limitations to significant information in biological electron microscopy as a result of radiation damage J. Ultrastruct. Res. 36 1971 466 482
    • (1971) J. Ultrastruct. Res. , vol.36 , pp. 466-482
    • Glaeser, R.M.1
  • 14
    • 0035876478 scopus 로고    scopus 로고
    • Finding and using local symmetry in identifying lower domain movements in hexon subunits of the herpes simplex virus type 1 B capsid
    • J. He, M.F. Schmid, Z.H. Zhou, F. Rixon, and W. Chiu Finding and using local symmetry in identifying lower domain movements in hexon subunits of the herpes simplex virus type 1 B capsid J. Mol. Biol. 309 2001 903 914
    • (2001) J. Mol. Biol. , vol.309 , pp. 903-914
    • He, J.1    Schmid, M.F.2    Zhou, Z.H.3    Rixon, F.4    Chiu, W.5
  • 15
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules
    • R. Henderson The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules Q. Rev. Biophys. 28 1995 171 193
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 171-193
    • Henderson, R.1
  • 16
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • R. Henderson, J.M. Baldwin, T.A. Ceska, F. Zemlin, E. Beckmann, and K.H. Downing Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy J. Mol. Biol. 213 1990 899 929
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 18
    • 0024961660 scopus 로고
    • Visualization of alpha-helices in tobacco mosaic virus by cryo-electron microscopy
    • T.W. Jeng, R.A. Crowther, G. Stubbs, and W. Chiu Visualization of alpha-helices in tobacco mosaic virus by cryo-electron microscopy J. Mol. Biol. 205 1989 251 257
    • (1989) J. Mol. Biol. , vol.205 , pp. 251-257
    • Jeng, T.W.1    Crowther, R.A.2    Stubbs, G.3    Chiu, W.4
  • 19
    • 0035906702 scopus 로고    scopus 로고
    • Bridging the information gap: Computational tools for intermediate resolution structure interpretation
    • W. Jiang, M.L. Baker, S.J. Ludtke, and W. Chiu Bridging the information gap: computational tools for intermediate resolution structure interpretation J. Mol. Biol. 308 2001 1033 1044
    • (2001) J. Mol. Biol. , vol.308 , pp. 1033-1044
    • Jiang, W.1    Baker, M.L.2    Ludtke, S.J.3    Chiu, W.4
  • 20
    • 0037313264 scopus 로고    scopus 로고
    • Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions
    • W. Jiang, Z. Li, Z. Zhang, M.L. Baker, P.E. Prevelige Jr., and W. Chiu Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions Nat. Struct. Biol. 10 2003 131 135
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 131-135
    • Jiang, W.1    Li, Z.2    Zhang, Z.3    Baker, M.L.4    Prevelige Jr., P.E.5    Chiu, W.6
  • 21
    • 0002608842 scopus 로고    scopus 로고
    • The procapsid to capsid transition in double-stranded DNA bacteriophages
    • W. Chiu R.M. Burnett R.L. Garcea Oxford Press New York
    • J. King, and W. Chiu The procapsid to capsid transition in double-stranded DNA bacteriophages W. Chiu R.M. Burnett R.L. Garcea Structural Biology of Viruses 1997 Oxford Press New York 288 311
    • (1997) Structural Biology of Viruses , pp. 288-311
    • King, J.1    Chiu, W.2
  • 22
    • 0041507094 scopus 로고    scopus 로고
    • A structural-informatics approach for mining beta-sheets: Locating sheets in intermediate-resolution density maps
    • Y. Kong, and J. Ma A structural-informatics approach for mining beta-sheets: locating sheets in intermediate-resolution density maps J. Mol. Biol. 332 2003 399 413
    • (2003) J. Mol. Biol. , vol.332 , pp. 399-413
    • Kong, Y.1    Ma, J.2
  • 23
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • W. Kühlbrandt, D.N. Wang, and Y. Fujiyoshi Atomic model of plant light-harvesting complex by electron crystallography Nature 367 1994 614 621
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 24
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semi-automated software for high resolution single particle reconstructions
    • S.J. Ludtke, P.R. Baldwin, and W. Chiu EMAN: Semi-automated software for high resolution single particle reconstructions J. Struct. Biol. 128 1999 82 97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 25
    • 3142538754 scopus 로고    scopus 로고
    • Seeing GroEL at 6 Å resolution by single particle electron cryomicroscopy
    • S.J. Ludtke, D.H. Chen, J.L. Song, D.T. Chuang, and W. Chiu Seeing GroEL at 6 Å resolution by single particle electron cryomicroscopy Structure 12 2004 1129 1136
    • (2004) Structure , vol.12 , pp. 1129-1136
    • Ludtke, S.J.1    Chen, D.H.2    Song, J.L.3    Chuang, D.T.4    Chiu, W.5
  • 26
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • A. Miyazawa, Y. Fujiyoshi, and N. Unwin Structure and gating mechanism of the acetylcholine receptor pore Nature 424 2003 949 955
    • (2003) Nature , vol.424 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 29
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • E. Nogales, S.G. Wolf, and K.H. Downing Structure of the alpha beta tubulin dimer by electron crystallography Nature 391 1998 199 203
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 32
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • P.B. Rosenthal, and R. Henderson Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy J. Mol. Biol. 333 2003 721 745
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 33
    • 0033813317 scopus 로고    scopus 로고
    • Conformational changes studied by cryo-electron microscopy
    • H.R. Saibil Conformational changes studied by cryo-electron microscopy Nat. Struct. Biol. 7 2000 711 714
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 711-714
    • Saibil, H.R.1
  • 34
    • 0031787022 scopus 로고    scopus 로고
    • 100,000 protein structures for the biologist
    • A. Sali 100,000 protein structures for the biologist Nat. Struct. Biol. 5 1998 1029 1032
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1029-1032
    • Sali, A.1
  • 35
    • 0041333147 scopus 로고    scopus 로고
    • NIH workshop on structural proteomics of biological complexes
    • A. Sali NIH workshop on structural proteomics of biological complexes Structure 11 2003 1043 1047
    • (2003) Structure , vol.11 , pp. 1043-1047
    • Sali, A.1
  • 36
    • 0028115630 scopus 로고
    • Three-dimensional structure of a single filament in the Limulus acrosomal bundle: Scruin binds to homologous helix-loop-beta motifs in actin
    • M.F. Schmid, J.M. Agris, J. Jakana, P. Matsudaira, and W. Chiu Three-dimensional structure of a single filament in the Limulus acrosomal bundle: scruin binds to homologous helix-loop-beta motifs in actin J. Cell Biol. 124 1994 341 350
    • (1994) J. Cell Biol. , vol.124 , pp. 341-350
    • Schmid, M.F.1    Agris, J.M.2    Jakana, J.3    Matsudaira, P.4    Chiu, W.5
  • 38
    • 0033585094 scopus 로고    scopus 로고
    • The three-dimensional structure of the Limulus acrosomal process: A dynamic actin bundle
    • M.B. Sherman, J. Jakana, S. Sun, P. Matsudaira, W. Chiu, and M.F. Schmid The three-dimensional structure of the Limulus acrosomal process: a dynamic actin bundle J. Mol. Biol. 294 1999 139 149
    • (1999) J. Mol. Biol. , vol.294 , pp. 139-149
    • Sherman, M.B.1    Jakana, J.2    Sun, S.3    Matsudaira, P.4    Chiu, W.5    Schmid, M.F.6
  • 39
    • 0034632864 scopus 로고    scopus 로고
    • Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
    • S. Subramaniam, and R. Henderson Molecular mechanism of vectorial proton translocation by bacteriorhodopsin Nature 406 2000 653 657
    • (2000) Nature , vol.406 , pp. 653-657
    • Subramaniam, S.1    Henderson, R.2
  • 40
    • 0026799361 scopus 로고
    • Molecular analysis of rice dwarf phytoreovirus segment S1: Interviral homology of the putative RNA-dependent RNA polymerase between plant- and animal-infecting reoviruses
    • N. Suzuki, M. Tanimura, Y. Watanabe, T. Kusano, Y. Kitagawa, N. Suda, H. Kudo, I. Uyeda, and E. Shikata Molecular analysis of rice dwarf phytoreovirus segment S1: interviral homology of the putative RNA-dependent RNA polymerase between plant- and animal-infecting reoviruses Virology 190 1992 240 247
    • (1992) Virology , vol.190 , pp. 240-247
    • Suzuki, N.1    Tanimura, M.2    Watanabe, Y.3    Kusano, T.4    Kitagawa, Y.5    Suda, N.6    Kudo, H.7    Uyeda, I.8    Shikata, E.9
  • 41
    • 0016431173 scopus 로고
    • Actin filaments in the acrosomal reaction of Limulus sperm
    • L.G. Tilney Actin filaments in the acrosomal reaction of Limulus sperm J. Cell Biol. 64 1975 289 310
    • (1975) J. Cell Biol. , vol.64 , pp. 289-310
    • Tilney, L.G.1
  • 42
    • 12844256969 scopus 로고    scopus 로고
    • Structural modeling of components in protein assemblies by comparative modeling and electron cryo-microscopy
    • M. Topf, M.L. Baker, B. John, W. Chiu, and A. Sali Structural modeling of components in protein assemblies by comparative modeling and electron cryo-microscopy J. Struct. Biol. 149 2005 191 203
    • (2005) J. Struct. Biol. , vol.149 , pp. 191-203
    • Topf, M.1    Baker, M.L.2    John, B.3    Chiu, W.4    Sali, A.5
  • 43
    • 0023090371 scopus 로고
    • Similarity measures between images
    • M. van Heel Similarity measures between images Ultramicroscopy 21 1987 95 100
    • (1987) Ultramicroscopy , vol.21 , pp. 95-100
    • Van Heel, M.1
  • 44
    • 0032779888 scopus 로고    scopus 로고
    • Quantitative fitting of atomic models into observed densities derived by electron microscopy
    • N. Volkmann, and D. Hanein Quantitative fitting of atomic models into observed densities derived by electron microscopy J. Struct. Biol. 125 1999 176 184
    • (1999) J. Struct. Biol. , vol.125 , pp. 176-184
    • Volkmann, N.1    Hanein, D.2
  • 45
    • 0035783173 scopus 로고    scopus 로고
    • Using situs for flexible and rigid-body fitting of multiresolution single-molecule data
    • W. Wriggers, and S. Birmanns Using situs for flexible and rigid-body fitting of multiresolution single-molecule data J. Struct. Biol. 133 2001 193 202
    • (2001) J. Struct. Biol. , vol.133 , pp. 193-202
    • Wriggers, W.1    Birmanns, S.2
  • 46
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • K. Yonekura, S. Maki-Yonekura, and K. Namba Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy Nature 424 2003 643 650
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 47
    • 0042827239 scopus 로고    scopus 로고
    • Determination of icosahedral virus structures by electron cryomicroscopy at subnanometer resolution
    • Z.H. Zhou, and W. Chiu Determination of icosahedral virus structures by electron cryomicroscopy at subnanometer resolution Adv. Protein Chem. 64 2003 93 124
    • (2003) Adv. Protein Chem. , vol.64 , pp. 93-124
    • Zhou, Z.H.1    Chiu, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.