메뉴 건너뛰기




Volumn 337, Issue 1, 2004, Pages 105-113

Structure of the Rotor of the Bacterial Flagellar Motor Revealed by Electron Cryomicroscopy and Single-particle Image Analysis

Author keywords

Bacterial flagellum; Basal body; Electron cryomicroscopy; Flagellar motor; Single particle image analysis

Indexed keywords

BACTERIAL PROTEIN; PROTEIN FLIF; PROTEIN FLIG; UNCLASSIFIED DRUG;

EID: 1442326719     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.01.034     Document Type: Article
Times cited : (135)

References (55)
  • 1
    • 0034728850 scopus 로고    scopus 로고
    • Constraints on models for the flagellar rotary motor
    • Berg H.C. Constraints on models for the flagellar rotary motor. Phil. Trans. Roy. Soc. ser. B. 355:2000;491-501.
    • (2000) Phil. Trans. Roy. Soc. Ser. B , vol.355 , pp. 491-501
    • Berg, H.C.1
  • 2
    • 0041673353 scopus 로고    scopus 로고
    • The rotary motor of bacterial flagella
    • Berg H.C. The rotary motor of bacterial flagella. Annu. Rev. Biochem. 72:2003;19-54.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 19-54
    • Berg, H.C.1
  • 3
    • 0030992385 scopus 로고    scopus 로고
    • Molecular architecture of bacterial flagellum
    • Namba K., Vonderviszt F. Molecular architecture of bacterial flagellum. Quart. Rev. Biophys. 30:1997;1-65.
    • (1997) Quart. Rev. Biophys. , vol.30 , pp. 1-65
    • Namba, K.1    Vonderviszt, F.2
  • 4
    • 0020410957 scopus 로고
    • Flagellar hook structures of Caulobacter and Salmonella and their relationship to filament structure
    • Wagenknecht T., DeRosier D.J., Aizawa S., Macnab R.M. Flagellar hook structures of Caulobacter and Salmonella and their relationship to filament structure. J. Mol. Biol. 162:1982;69-87.
    • (1982) J. Mol. Biol. , vol.162 , pp. 69-87
    • Wagenknecht, T.1    Derosier, D.J.2    Aizawa, S.3    MacNab, R.M.4
  • 5
    • 0028093390 scopus 로고
    • Roles of FliK and FlhB in determination of flagellar hook length in Salmonella typhimurium
    • Hirano T., Yamaguchi S., Oosawa K., Aizawa S. Roles of FliK and FlhB in determination of flagellar hook length in Salmonella typhimurium. J. Bacteriol. 176:1994;5439-5449.
    • (1994) J. Bacteriol. , vol.176 , pp. 5439-5449
    • Hirano, T.1    Yamaguchi, S.2    Oosawa, K.3    Aizawa, S.4
  • 6
    • 0026792838 scopus 로고
    • M ring, S ring and proximal rod of the flagellar basal body of Salmonella typhimurium are composed of subunits of a single protein, FliF
    • Ueno T., Oosawa K., Aizawa S. M ring, S ring and proximal rod of the flagellar basal body of Salmonella typhimurium are composed of subunits of a single protein, FliF. J. Mol. Biol. 227:1992;672-677.
    • (1992) J. Mol. Biol. , vol.227 , pp. 672-677
    • Ueno, T.1    Oosawa, K.2    Aizawa, S.3
  • 7
    • 0014974951 scopus 로고
    • Attachment of flagellar basal bodies to the cell envelope: Specific attachment to the outer, lipopolysaccharide membrane and the cytoplasmic membrane
    • DePamphilis M.L., Adler J. Attachment of flagellar basal bodies to the cell envelope: specific attachment to the outer, lipopolysaccharide membrane and the cytoplasmic membrane. J. Bacteriol. 105:1971;396-407.
    • (1971) J. Bacteriol. , vol.105 , pp. 396-407
    • Depamphilis, M.L.1    Adler, J.2
  • 8
    • 0032568636 scopus 로고    scopus 로고
    • Electrostatic interactions between rotor and stator in the bacterial flagellar motor
    • Zhou J., Lloyd S.A., Blair D.F. Electrostatic interactions between rotor and stator in the bacterial flagellar motor. Proc. Natl Acad. Sci. USA. 95:1998;6436-6441.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6436-6441
    • Zhou, J.1    Lloyd, S.A.2    Blair, D.F.3
  • 9
    • 0026740392 scopus 로고
    • Localization of the Salmonella typhimurium flagellar switch protein FliG to the cytoplasmic M-ring face of the basal body
    • Francis N.R., Irikura V.M., Yamaguchi S., DeRosier D.J., Macnab R.M. Localization of the Salmonella typhimurium flagellar switch protein FliG to the cytoplasmic M-ring face of the basal body. Proc. Natl Acad. Sci. USA. 89:1992;6304-6308.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 6304-6308
    • Francis, N.R.1    Irikura, V.M.2    Yamaguchi, S.3    Derosier, D.J.4    MacNab, R.M.5
  • 10
    • 0023750050 scopus 로고
    • Effects of mot gene expression on the structure of the flagellar motor
    • Khan S., Dapice M., Reese T.S. Effects of mot gene expression on the structure of the flagellar motor. J. Mol. Biol. 202:1988;575-584.
    • (1988) J. Mol. Biol. , vol.202 , pp. 575-584
    • Khan, S.1    Dapice, M.2    Reese, T.S.3
  • 11
    • 0025058346 scopus 로고
    • The MotA protein of E. coli is a proton-conducting component of the flagellar motor
    • Blair D.F., Berg H.C. The MotA protein of E. coli is a proton-conducting component of the flagellar motor. Cell. 60:1990;439-449.
    • (1990) Cell , vol.60 , pp. 439-449
    • Blair, D.F.1    Berg, H.C.2
  • 12
    • 0025718616 scopus 로고
    • Evidence for interactions between MotA and MotB, torque-generating elements of the flagellar motor of Escherichia coli
    • Stolz B., Berg H.C. Evidence for interactions between MotA and MotB, torque-generating elements of the flagellar motor of Escherichia coli. J. Bacteriol. 173:1991;7033-7037.
    • (1991) J. Bacteriol. , vol.173 , pp. 7033-7037
    • Stolz, B.1    Berg, H.C.2
  • 13
    • 0024286468 scopus 로고
    • Bacterial motility: Membrane topology of the Escherichia coli MotB protein
    • Chun S.Y., Parkinson J.S. Bacterial motility: membrane topology of the Escherichia coli MotB protein. Science. 239:1988;276-278.
    • (1988) Science , vol.239 , pp. 276-278
    • Chun, S.Y.1    Parkinson, J.S.2
  • 14
    • 0033614958 scopus 로고    scopus 로고
    • Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor
    • Lloyd S.A., Whitby F.G., Blair D.F., Hill C.P. Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor. Nature. 400:1999;472-475.
    • (1999) Nature , vol.400 , pp. 472-475
    • Lloyd, S.A.1    Whitby, F.G.2    Blair, D.F.3    Hill, C.P.4
  • 15
    • 0030776508 scopus 로고    scopus 로고
    • Residues of the cytoplasmic domain of MotA essential for torque generation in the bacterial flagellar motor
    • Zhou J., Blair D.F. Residues of the cytoplasmic domain of MotA essential for torque generation in the bacterial flagellar motor. J. Mol. Biol. 273:1997;428-439.
    • (1997) J. Mol. Biol. , vol.273 , pp. 428-439
    • Zhou, J.1    Blair, D.F.2
  • 16
  • 17
    • 0034460297 scopus 로고    scopus 로고
    • How signals are heard during bacterial chemotaxis: Protein-protein interactions in sensory signal propagation
    • Bren A., Eisenbach M. How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation. J. Bacteriol. 182:2000;6865-6873.
    • (2000) J. Bacteriol. , vol.182 , pp. 6865-6873
    • Bren, A.1    Eisenbach, M.2
  • 18
    • 0025374078 scopus 로고
    • Additional structures associated with bacterial flagellar basal body
    • Driks A., DeRosier D.J. Additional structures associated with bacterial flagellar basal body. J. Mol. Biol. 211:1990;669-672.
    • (1990) J. Mol. Biol. , vol.211 , pp. 669-672
    • Driks, A.1    Derosier, D.J.2
  • 19
    • 0031023773 scopus 로고    scopus 로고
    • Assembly of the switch complex onto the MS ring complex of Salmonella typhimurium does not require any other flagellar proteins
    • Kubori T., Yamaguchi S., Aizawa S. Assembly of the switch complex onto the MS ring complex of Salmonella typhimurium does not require any other flagellar proteins. J. Bacteriol. 179:1997;813-817.
    • (1997) J. Bacteriol. , vol.179 , pp. 813-817
    • Kubori, T.1    Yamaguchi, S.2    Aizawa, S.3
  • 20
    • 0022899744 scopus 로고
    • Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimurium
    • Yamaguchi S., Aizawa S., Kihara M., Isomura M., Jones C.J., Macnab R.M. Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimurium. J. Bacteriol. 168:1986;1172-1179.
    • (1986) J. Bacteriol. , vol.168 , pp. 1172-1179
    • Yamaguchi, S.1    Aizawa, S.2    Kihara, M.3    Isomura, M.4    Jones, C.J.5    MacNab, R.M.6
  • 21
    • 0014620624 scopus 로고
    • Genetics and chemistry of bacterial flagella
    • Iino T. Genetics and chemistry of bacterial flagella. Bacteriol. Rev. 33:1969;454-475.
    • (1969) Bacteriol. Rev. , vol.33 , pp. 454-475
    • Iino, T.1
  • 22
    • 0030023488 scopus 로고    scopus 로고
    • Flagellar assembly in Salmonella typhimurium
    • Aizawa S.I. Flagellar assembly in Salmonella typhimurium. Mol. Microbiol. 19:1996;1-5.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1-5
    • Aizawa, S.I.1
  • 23
    • 0014939798 scopus 로고
    • Bacterial flagella: Polarity of elongation
    • Emerson S.U., Tokuyasu K., Simon M.I. Bacterial flagella: polarity of elongation. Science. 169:1970;190-192.
    • (1970) Science , vol.169 , pp. 190-192
    • Emerson, S.U.1    Tokuyasu, K.2    Simon, M.I.3
  • 24
    • 0032698478 scopus 로고    scopus 로고
    • The bacterial flagellum: Reversible rotary propeller and type III export apparatus
    • Macnab R.M. The bacterial flagellum: reversible rotary propeller and type III export apparatus. J. Bacteriol. 181:1999;7149-7153.
    • (1999) J. Bacteriol. , vol.181 , pp. 7149-7153
    • MacNab, R.M.1
  • 25
    • 0242693166 scopus 로고    scopus 로고
    • How bacteria assemble flagella
    • Macnab R.M. How bacteria assemble flagella. Annu. Rev. Biochem. 57:2003;77-100.
    • (2003) Annu. Rev. Biochem. , vol.57 , pp. 77-100
    • MacNab, R.M.1
  • 26
    • 0033059596 scopus 로고    scopus 로고
    • Components of the Salmonella flagellar export apparatus and classification of export substrates
    • Minamino T., Macnab R.M. Components of the Salmonella flagellar export apparatus and classification of export substrates. J. Bacteriol. 181:1999;1388-1394.
    • (1999) J. Bacteriol. , vol.181 , pp. 1388-1394
    • Minamino, T.1    MacNab, R.M.2
  • 28
    • 0032562678 scopus 로고    scopus 로고
    • Supramolecular structure of the Salmonella typhimurium type III protein secretion system
    • Kubori T., Matsushima Y., Nakamura D., Uralil J., Lara-Tejero M., Sukhan A., et al. Supramolecular structure of the Salmonella typhimurium type III protein secretion system. Science. 280:1998;602-605.
    • (1998) Science , vol.280 , pp. 602-605
    • Kubori, T.1    Matsushima, Y.2    Nakamura, D.3    Uralil, J.4    Lara-Tejero, M.5    Sukhan, A.6
  • 29
    • 0028951802 scopus 로고
    • The hrp gene locus of Pseudomonas solanacearum, which controls the production of a type III secretion system, encodes eight proteins related to components of the bacterial flagellar biogenesis complex
    • Van Gijsegem F., Gough C., Zischek C., Niqueux E., Arlat M., Genin S., et al. The hrp gene locus of Pseudomonas solanacearum, which controls the production of a type III secretion system, encodes eight proteins related to components of the bacterial flagellar biogenesis complex. Mol. Microbiol. 15:1995;1095-1114.
    • (1995) Mol. Microbiol. , vol.15 , pp. 1095-1114
    • Van Gijsegem, F.1    Gough, C.2    Zischek, C.3    Niqueux, E.4    Arlat, M.5    Genin, S.6
  • 30
    • 0024394063 scopus 로고
    • L-, P-, and M-ring proteins of the flagellar basal body of Salmonella typhimurium: Gene sequences and deduced protein sequences
    • Jones C.J., Homma M., Macnab R.M. L-, P-, and M-ring proteins of the flagellar basal body of Salmonella typhimurium: gene sequences and deduced protein sequences. J. Bacteriol. 171:1989;3890-3900.
    • (1989) J. Bacteriol. , vol.171 , pp. 3890-3900
    • Jones, C.J.1    Homma, M.2    MacNab, R.M.3
  • 31
    • 0028210772 scopus 로고
    • Domain structures of the MS ring component protein (FliF) of the flagellar basal body of Salmonella typhimurium
    • Ueno T., Oosawa K., Aizawa S. Domain structures of the MS ring component protein (FliF) of the flagellar basal body of Salmonella typhimurium. J. Mol. Biol. 236:1994;546-555.
    • (1994) J. Mol. Biol. , vol.236 , pp. 546-555
    • Ueno, T.1    Oosawa, K.2    Aizawa, S.3
  • 32
    • 0025272595 scopus 로고
    • Stoichiometric analysis of the flagellar hook-(basal-body) complex of Salmonella typhimurium
    • Jones C.J., Macnab R.M., Okino H., Aizawa S. Stoichiometric analysis of the flagellar hook-(basal-body) complex of Salmonella typhimurium. J. Mol. Biol. 212:1990;377-387.
    • (1990) J. Mol. Biol. , vol.212 , pp. 377-387
    • Jones, C.J.1    MacNab, R.M.2    Okino, H.3    Aizawa, S.4
  • 33
    • 0026752989 scopus 로고
    • Morphological pathway of flagellar assembly in Salmonella typhimurium
    • Kubori T., Shimamoto N., Yamaguchi S., Namba K., Aizawa S. Morphological pathway of flagellar assembly in Salmonella typhimurium. J. Mol. Biol. 226:1992;433-446.
    • (1992) J. Mol. Biol. , vol.226 , pp. 433-446
    • Kubori, T.1    Shimamoto, N.2    Yamaguchi, S.3    Namba, K.4    Aizawa, S.5
  • 34
    • 0028274712 scopus 로고
    • Isolation, characterization and structure of bacterial flagellar motors containing the switch complex
    • Francis N.R., Sosinsky G.E., Thomas D., DeRosier D.J. Isolation, characterization and structure of bacterial flagellar motors containing the switch complex. J. Mol. Biol. 235:1994;1261-1270.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1261-1270
    • Francis, N.R.1    Sosinsky, G.E.2    Thomas, D.3    Derosier, D.J.4
  • 35
    • 0032464279 scopus 로고    scopus 로고
    • A structural feature in the central channel of the bacterial flagellar FliF ring complex is implicated in type III protein export
    • Suzuki H., Yonekura K., Murata K., Hirai T., Oosawa K., Namba K. A structural feature in the central channel of the bacterial flagellar FliF ring complex is implicated in type III protein export. J. Struct. Biol. 124:1998;104-114.
    • (1998) J. Struct. Biol. , vol.124 , pp. 104-114
    • Suzuki, H.1    Yonekura, K.2    Murata, K.3    Hirai, T.4    Oosawa, K.5    Namba, K.6
  • 36
    • 0029360470 scopus 로고
    • Improved methods for determination of rotational symmetries in macromolecules
    • Kocsis E., Cerritelli M.E., Trus B.L., Cheng N., Steven A.C. Improved methods for determination of rotational symmetries in macromolecules. Ultramicroscopy. 60:1995;219-228.
    • (1995) Ultramicroscopy , vol.60 , pp. 219-228
    • Kocsis, E.1    Cerritelli, M.E.2    Trus, B.L.3    Cheng, N.4    Steven, A.C.5
  • 37
    • 0033621062 scopus 로고    scopus 로고
    • Rotational symmetry of the C ring and a mechanism for the flagellar rotary motor
    • Thomas D.R., Morgan D.G., DeRosier D.J. Rotational symmetry of the C ring and a mechanism for the flagellar rotary motor. Proc. Natl Acad. Sci. USA. 96:1999;10134-10139.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 10134-10139
    • Thomas, D.R.1    Morgan, D.G.2    Derosier, D.J.3
  • 38
    • 12244302174 scopus 로고    scopus 로고
    • Variable symmetry in Salmonella typhimurium flagellar motors
    • Young H.S., Dang H., Lai Y., DeRosier D.J., Khan S. Variable symmetry in Salmonella typhimurium flagellar motors. Biophys. J. 84:2003;571-577.
    • (2003) Biophys. J. , vol.84 , pp. 571-577
    • Young, H.S.1    Dang, H.2    Lai, Y.3    Derosier, D.J.4    Khan, S.5
  • 40
    • 0025367437 scopus 로고
    • Flagellar hook and hook-associated proteins of Salmonella typhimurium and their relationship to other axial components of the flagellum
    • Homma M., DeRosier D.J., Macnab R.M. Flagellar hook and hook-associated proteins of Salmonella typhimurium and their relationship to other axial components of the flagellum. J. Mol. Biol. 213:1990;819-832.
    • (1990) J. Mol. Biol. , vol.213 , pp. 819-832
    • Homma, M.1    Derosier, D.J.2    MacNab, R.M.3
  • 41
    • 0025115312 scopus 로고
    • FlgB, FlgC, FlgF and FlgG. a family of structurally related proteins in the flagellar basal body of Salmonella typhimurium
    • Homma M., Kutsukake K., Hasebe M., Iino T., Macnab R.M. FlgB, FlgC, FlgF and FlgG. A family of structurally related proteins in the flagellar basal body of Salmonella typhimurium. J. Mol. Biol. 211:1990;465-477.
    • (1990) J. Mol. Biol. , vol.211 , pp. 465-477
    • Homma, M.1    Kutsukake, K.2    Hasebe, M.3    Iino, T.4    MacNab, R.M.5
  • 42
    • 0015506131 scopus 로고
    • Structure of straight flagella from a mutant Salmonella
    • O'Brien E.J., Bennett P.M. Structure of straight flagella from a mutant Salmonella. J. Mol. Biol. 70:1972;133-152.
    • (1972) J. Mol. Biol. , vol.70 , pp. 133-152
    • O'Brien, E.J.1    Bennett, P.M.2
  • 43
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura K., Maki-Yonekura S., Namba K. 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
  • 44
    • 0029042213 scopus 로고
    • Structure of bacterial flagellar filaments at 11 Å resolution: Packing of the alpha-helices
    • Morgan D.G., Owen C., Melanson L.A., DeRosier D.J. Structure of bacterial flagellar filaments at 11 Å resolution: packing of the alpha-helices. J. Mol. Biol. 249:1995;88-110.
    • (1995) J. Mol. Biol. , vol.249 , pp. 88-110
    • Morgan, D.G.1    Owen, C.2    Melanson, L.A.3    Derosier, D.J.4
  • 45
    • 0029039662 scopus 로고
    • The structure of the R-type straight flagellar filament of Salmonella at 9 Å resolution by electron cryomicroscopy
    • Mimori Y., Yamashita I., Murata K., Fujiyoshi Y., Yonekura K., Toyoshima C., Namba K. The structure of the R-type straight flagellar filament of Salmonella at 9 Å resolution by electron cryomicroscopy. J. Mol. Biol. 249:1995;69-87.
    • (1995) J. Mol. Biol. , vol.249 , pp. 69-87
    • Mimori, Y.1    Yamashita, I.2    Murata, K.3    Fujiyoshi, Y.4    Yonekura, K.5    Toyoshima, C.6    Namba, K.7
  • 46
    • 0024563358 scopus 로고
    • Release of flagellar filament-hook-rod complex by a Salmonella typhimurium mutant defective in the M ring of the basal body
    • Okino H., Isomura M., Yamaguchi S., Magariyama Y., Kudo S., Aizawa S.I. Release of flagellar filament-hook-rod complex by a Salmonella typhimurium mutant defective in the M ring of the basal body. J. Bacteriol. 171:1989;2075-2082.
    • (1989) J. Bacteriol. , vol.171 , pp. 2075-2082
    • Okino, H.1    Isomura, M.2    Yamaguchi, S.3    Magariyama, Y.4    Kudo, S.5    Aizawa, S.I.6
  • 47
    • 0030701512 scopus 로고    scopus 로고
    • The FliP and FliR proteins of Salmonella typhimurium, putative components of the type III flagellar export apparatus, are located in the flagellar basal body
    • Fan F., Ohnishi K., Francis N.R., Macnab R.M. The FliP and FliR proteins of Salmonella typhimurium, putative components of the type III flagellar export apparatus, are located in the flagellar basal body. Mol. Microbiol. 26:1997;1035-1046.
    • (1997) Mol. Microbiol. , vol.26 , pp. 1035-1046
    • Fan, F.1    Ohnishi, K.2    Francis, N.R.3    MacNab, R.M.4
  • 48
    • 0028000731 scopus 로고
    • Structure of viral connectors and their function in bacteriophage assembly and DNA packaging
    • Valpuesta J.M., Carrascosa J.L. Structure of viral connectors and their function in bacteriophage assembly and DNA packaging. Quart. Rev. Biophys. 27:1994;107-155.
    • (1994) Quart. Rev. Biophys. , vol.27 , pp. 107-155
    • Valpuesta, J.M.1    Carrascosa, J.L.2
  • 50
    • 0037451286 scopus 로고    scopus 로고
    • Structure of a viral DNA gatekeeper at 10 Å resolution by cryo-electron microscopy
    • Orlova E.V., Gowen B., Droge A., Stiege A., Weise F., Lurz R., et al. Structure of a viral DNA gatekeeper at 10 Å resolution by cryo-electron microscopy. EMBO J. 22:2003;1255-1262.
    • (2003) EMBO J. , vol.22 , pp. 1255-1262
    • Orlova, E.V.1    Gowen, B.2    Droge, A.3    Stiege, A.4    Weise, F.5    Lurz, R.6
  • 51
    • 0039538633 scopus 로고
    • Symmetry mismatch and DNA packaging in large bacteriophages
    • Hendrix R.W. Symmetry mismatch and DNA packaging in large bacteriophages. Proc. Natl Acad. Sci. USA. 75:1978;4779-4783.
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 4779-4783
    • Hendrix, R.W.1
  • 52
    • 0029978352 scopus 로고    scopus 로고
    • Geometry of the flagellar motor in the cytoplasmic membrane of Salmonella typhimurium as determined by stereo-photogrammetry of quick-freeze deep-etch replica images
    • Katayama E., Shiraishi T., Oosawa K., Baba N., Aizawa S. Geometry of the flagellar motor in the cytoplasmic membrane of Salmonella typhimurium as determined by stereo-photogrammetry of quick-freeze deep-etch replica images. J. Mol. Biol. 255:1996;458-475.
    • (1996) J. Mol. Biol. , vol.255 , pp. 458-475
    • Katayama, E.1    Shiraishi, T.2    Oosawa, K.3    Baba, N.4    Aizawa, S.5
  • 53
    • 0031583477 scopus 로고    scopus 로고
    • Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 Å resolution by electron cryomicroscopy and angular reconstitution
    • Orlova E.V., Dube P., Harris J.R., Beckman E., Zemlin F., Markl J., van Heel M. Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 Å resolution by electron cryomicroscopy and angular reconstitution. J. Mol. Biol. 271:1997;417-437.
    • (1997) J. Mol. Biol. , vol.271 , pp. 417-437
    • Orlova, E.V.1    Dube, P.2    Harris, J.R.3    Beckman, E.4    Zemlin, F.5    Markl, J.6    Van Heel, M.7
  • 54
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., Chiu W. EMAN: semiautomated 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
  • 55
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116:1996;190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.