메뉴 건너뛰기




Volumn 82, Issue , 2011, Pages 101-121

Future prospects

Author keywords

Cryo electron microscopy; Electron tomography; Protein Data Bank; Structure validation

Indexed keywords


EID: 79955005349     PISSN: 18761623     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-386507-6.00005-1     Document Type: Chapter
Times cited : (8)

References (91)
  • 1
    • 0032052907 scopus 로고    scopus 로고
    • Cryo-negative staining
    • DOI 10.1016/S0968-4328(97)00068-1, PII S0968432897000681
    • M. Adrian, J. Dubochet, S.D. Fuller, and J.R. Harris Cryo-negative staining Micron 29 1998 145 160 (Pubitemid 28348505)
    • (1998) Micron , vol.29 , Issue.2-3 , pp. 145-160
    • Adrian, M.1    Dubochet, J.2    Fuller, S.D.3    Harris, J.R.4
  • 2
    • 0032712359 scopus 로고    scopus 로고
    • Adding the third dimension to virus life cycles: Three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs
    • T.S. Baker, N.H. Olson, and S.D. Fuller Adding the third dimension to virus life cycles: three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs Microbiol. Mol. Biol. Rev. 63 1999 862 922
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 862-922
    • Baker, T.S.1    Olson, N.H.2    Fuller, S.D.3
  • 4
    • 0004290179 scopus 로고    scopus 로고
    • A 9 resolution X-ray crystallographic map of the large ribosomal subunit
    • N. Ban, B. Freeborn, P. Nissen, P. Penczek, R.A. Grassucci, and R. Sweet A 9 resolution X-ray crystallographic map of the large ribosomal subunit Cell 93 1998 1105 1116
    • (1998) Cell , vol.93 , pp. 1105-1116
    • Ban, N.1    Freeborn, B.2    Nissen, P.3    Penczek, P.4    Grassucci, R.A.5    Sweet, R.6
  • 6
    • 0041676176 scopus 로고
    • A numerical method for two-dimensional Fourier synthesis
    • C.A. Beevers, and H. Lipson A numerical method for two-dimensional Fourier synthesis Nature 137 1936 825 826
    • (1936) Nature , vol.137 , pp. 825-826
    • Beevers, C.A.1    Lipson, H.2
  • 8
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • DOI 10.1038/386088a0
    • B. Bttcher, S.A. Wynne, and R.A. Crowther Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy Nature 386 1997 88 91 (Pubitemid 27130926)
    • (1997) Nature , vol.386 , Issue.6620 , pp. 88-91
    • Bottcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 9
    • 0000573861 scopus 로고
    • The structure of some crystals as indicated by their diffraction of X-rays
    • W.L. Bragg The structure of some crystals as indicated by their diffraction of X-rays Proc. R. Soc. Lond. A89 1913 248 277
    • (1913) Proc. R. Soc. Lond. , vol.89 , pp. 248-277
    • Bragg, W.L.1
  • 10
    • 0345249062 scopus 로고
    • The determination of parameters in crystal structures by means of Fourier series
    • W.L. Bragg The determination of parameters in crystal structures by means of Fourier series Proc. R. Soc. Lond. A123 1929 537 559
    • (1929) Proc. R. Soc. Lond. , vol.123 , pp. 537-559
    • Bragg, W.L.1
  • 11
    • 33644806492 scopus 로고    scopus 로고
    • The mechanism of HIV-1 core assembly: Insights from three-dimensional reconstructions of authentic virions
    • DOI 10.1016/j.str.2005.09.010, PII S0969212605003898
    • J.A. Briggs, K. Grunewald, B. Glass, F. Forster, H.G. Krausslich, and S.D. Fuller The mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions Structure 14 2006 15 20 (Pubitemid 43350069)
    • (2006) Structure , vol.14 , Issue.1 , pp. 15-20
    • Briggs, J.A.G.1    Grunewald, K.2    Glass, B.3    Forster, F.4    Krausslich, H.-G.5    Fuller, S.D.6
  • 12
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • A.T. Brnger Free R value: a novel statistical quantity for assessing the accuracy of crystal structures Nature 355 1992 472 475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brnger, A.T.1
  • 14
    • 70350347088 scopus 로고    scopus 로고
    • Structural basis for the preferential recognition of immature flaviviruses by a fusion-loop antibody
    • M.V. Cherrier, B. Kaufmann, G.E. Nybakken, S.-M. Lok, J.T. Warren, and B.R. Chen Structural basis for the preferential recognition of immature flaviviruses by a fusion-loop antibody EMBO J. 28 2009 3269 3276
    • (2009) EMBO J. , vol.28 , pp. 3269-3276
    • Cherrier, M.V.1    Kaufmann, B.2    Nybakken, G.E.3    Lok, S.-M.4    Warren, J.T.5    Chen, B.R.6
  • 15
    • 77955088000 scopus 로고    scopus 로고
    • 4.6 Cryo-EM reconstruction of tobacco mosaic virus from images recorded at 300 keV on a 4k × 4k CCD camera
    • D.K. Clare, and E.V. Orlova 4.6 Cryo-EM reconstruction of tobacco mosaic virus from images recorded at 300 keV on a 4k × 4k CCD camera J. Struct. Biol. 171 2010 303 308
    • (2010) J. Struct. Biol. , vol.171 , pp. 303-308
    • Clare, D.K.1    Orlova, E.V.2
  • 16
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • DOI 10.1038/386091a0
    • J.F. Conway, N. Cheng, A. Zlotnick, P.T. Wingfield, S.J. Stahl, and A.C. Steven Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy Nature 386 1997 91 94 (Pubitemid 27130927)
    • (1997) Nature , vol.386 , Issue.6620 , pp. 91-94
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Wingfield, P.T.4    Stahl, S.J.5    Steven, A.C.6
  • 17
    • 0542431399 scopus 로고
    • X-ray crystallographic studies of compounds of biochemical interest
    • D. Crowfoot X-ray crystallographic studies of compounds of biochemical interest Annu. Rev. Biochem. 17 1948 115 146
    • (1948) Annu. Rev. Biochem. , vol.17 , pp. 115-146
    • Crowfoot, D.1
  • 18
    • 0015441377 scopus 로고
    • Three-dimensional image reconstructions of some small spherical viruses
    • R.A. Crowther, and L.A. Amos Three-dimensional image reconstructions of some small spherical viruses Cold Spring Harb. Symp. Quant. Biol. 36 1972 489 494
    • (1972) Cold Spring Harb. Symp. Quant. Biol. , vol.36 , pp. 489-494
    • Crowther, R.A.1    Amos, L.A.2
  • 19
    • 0014930077 scopus 로고
    • Three-dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs
    • R.A. Crowther, L.A. Amos, J.T. Finch, D.J. DeRosier, and A. Klug Three-dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs Nature 226 1970 421 425
    • (1970) Nature , vol.226 , pp. 421-425
    • Crowther, R.A.1    Amos, L.A.2    Finch, J.T.3    Derosier, D.J.4    Klug, A.5
  • 21
    • 61849092662 scopus 로고    scopus 로고
    • Practical factors affecting the performance of a thin-film phase plate for transmission electron microscopy
    • R. Danev, R.M. Glaeser, and K. Nagayama Practical factors affecting the performance of a thin-film phase plate for transmission electron microscopy Ultramicroscopy 109 2009 312 325
    • (2009) Ultramicroscopy , vol.109 , pp. 312-325
    • Danev, R.1    Glaeser, R.M.2    Nagayama, K.3
  • 22
    • 0036427905 scopus 로고    scopus 로고
    • Cryo-negative staining reduces electron-beam sensitivity of vitrified biological particles
    • DOI 10.1016/S1047-8477(02)00035-7, PII S1047847702000357
    • S. De Carlo, C. El-Bez, C. Alvarez-Ra, J. Borge, and J. Dubochet Cryo-negative staining reduces electron-beam sensitivity of vitrified biological particles J. Struct. Biol. 138 2002 216 226 (Pubitemid 35304468)
    • (2002) Journal of Structural Biology , vol.138 , Issue.3 , pp. 216-226
    • De Carlo, S.1    El-Bez, C.2    Alvarez-Rua, C.3    Borge, J.4    Dubochet, J.5
  • 23
    • 78649808726 scopus 로고    scopus 로고
    • Negative staining and cryo-negative staining of macromolecules and viruses for TEM
    • S. De Carlo, and J.R. Harris Negative staining and cryo-negative staining of macromolecules and viruses for TEM Micron 42 2011 117 131
    • (2011) Micron , vol.42 , pp. 117-131
    • De Carlo, S.1    Harris, J.R.2
  • 24
    • 0000668797 scopus 로고
    • Reconstruction of three dimensional structures from electron micrographs
    • D.J. De Rosier, and A. Klug Reconstruction of three dimensional structures from electron micrographs Nature 217 1968 130 134
    • (1968) Nature , vol.217 , pp. 130-134
    • De Rosier, D.J.1    Klug, A.2
  • 27
    • 0012172222 scopus 로고
    • N.V.A. Oosthoek's Uitgeversmaatschappij for the International Union of Crystallography Utrecht, The Netherlands
    • P.P. Ewald Fifty Years of X-Ray Diffraction 1962 N.V.A. Oosthoek's Uitgeversmaatschappij for the International Union of Crystallography Utrecht, The Netherlands
    • (1962) Fifty Years of X-Ray Diffraction
    • Ewald, P.P.1
  • 30
    • 0024917928 scopus 로고
    • Image analysis of single macromolecules
    • J. Frank Image analysis of single macromolecules Electron Microsc. Rev. 2 1989 53 74
    • (1989) Electron Microsc. Rev. , vol.2 , pp. 53-74
    • Frank, J.1
  • 32
    • 55249110450 scopus 로고    scopus 로고
    • Three-dimensional organization of Rift Valley fever virus revealed by cryoelectron tomography
    • DOI 10.1128/JVI.01191-08
    • A.N. Freiberg, M.B. Sherman, M.C. Morais, M.R. Holbrok, and S.J. Watowich Three-dimensional organization of Rift Valley fever virus revealed by cryo-electron tomography J. Virol. 82 2008 10341 10348 (Pubitemid 352691144)
    • (2008) Journal of Virology , vol.82 , Issue.21 , pp. 10341-10348
    • Freiberg, A.N.1    Sherman, M.B.2    Morais, M.C.3    Holbrook, M.R.4    Watowich, S.J.5
  • 36
    • 77956114530 scopus 로고    scopus 로고
    • Virology. Looking inside adenovirus
    • S.C. Harrison Virology. Looking inside adenovirus Science 329 2010 1026 1027
    • (2010) Science , vol.329 , pp. 1026-1027
    • Harrison, S.C.1
  • 38
    • 0014433959 scopus 로고
    • Electron microscopy of unstained biological material: The polytropic montage
    • R.G. Hart Electron microscopy of unstained biological material: the polytropic montage Science 159 1968 1464 1467
    • (1968) Science , vol.159 , pp. 1464-1467
    • Hart, R.G.1
  • 39
    • 77954384451 scopus 로고    scopus 로고
    • Automatic coarse-alignment for TEM tilt series of rod-shaped specimens collected with a full angular range
    • M. Hayashida, S. Terauchi, and T. Fujimoto Automatic coarse-alignment for TEM tilt series of rod-shaped specimens collected with a full angular range Micron 41 2010 540 545
    • (2010) Micron , vol.41 , pp. 540-545
    • Hayashida, M.1    Terauchi, S.2    Fujimoto, T.3
  • 40
    • 72849128417 scopus 로고    scopus 로고
    • Interactions and oligomerization of hantavirus glycoproteins
    • J. Hepojoki, T. Strandin, A. Vaheri, and H. Lankinen Interactions and oligomerization of hantavirus glycoproteins J. Virol. 84 2010 227 242
    • (2010) J. Virol. , vol.84 , pp. 227-242
    • Hepojoki, J.1    Strandin, T.2    Vaheri, A.3    Lankinen, H.4
  • 43
    • 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 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
  • 44
    • 0016327614 scopus 로고
    • Three-dimensional reconstruction of individual negatively stained yeast fatty-acid synthetase molecules from tilt series in the electron microscope
    • W. Hoppe, J. Gassmann, N. Hunsmann, H.J. Schramm, and M. Sturm Three-dimensional reconstruction of individual negatively stained yeast fatty-acid synthetase molecules from tilt series in the electron microscope Hoppe-Seyler's Z. Physiol. Chem. 355 1974 1482 1487
    • (1974) Hoppe-Seyler's Z. Physiol. Chem. , vol.355 , pp. 1482-1487
    • Hoppe, W.1    Gassmann, J.2    Hunsmann, N.3    Schramm, H.J.4    Sturm, M.5
  • 45
    • 77951477375 scopus 로고    scopus 로고
    • Electron cryotomography of Tula hantavirus suggests a unique assembly paradigm for enveloped viruses
    • J.T. Huiskonen, J. Hepojoki, P. Laurinmki, A. Vaheri, H. Lankinen, and S.J. Butcher Electron cryotomography of Tula hantavirus suggests a unique assembly paradigm for enveloped viruses J. Virol. 84 2010 4889 4897
    • (2010) J. Virol. , vol.84 , pp. 4889-4897
    • Huiskonen, J.T.1    Hepojoki, J.2    Laurinmki, P.3    Vaheri, A.4    Lankinen, H.5    Butcher, S.J.6
  • 47
    • 39849102970 scopus 로고    scopus 로고
    • Backbone structure of the infectious ε15 virus capsid revealed by electron cryomicroscopy
    • DOI 10.1038/nature06665, PII NATURE06665
    • W. Jiang, M.L. Baker, J. Jakana, P.R. Weigele, J. King, and W. Chiu Backbone structure of the infectious ε15 virus capsid revealed by electron cryomicroscopy Nature 451 2008 1130 1134 (Pubitemid 351317451)
    • (2008) Nature , vol.451 , Issue.7182 , pp. 1130-1134
    • Jiang, W.1    Baker, M.L.2    Jakana, J.3    Weigele, P.R.4    King, J.5    Chiu, W.6
  • 48
    • 77951982148 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of West Nile virus
    • B. Kaufmann, P. Plevka, R.J. Kuhn, and M.G. Rossmann Crystallization and preliminary X-ray diffraction analysis of West Nile virus Acta Crystallogr. F66 2010 558 562
    • (2010) Acta Crystallogr. , vol.66 , pp. 558-562
    • Kaufmann, B.1    Plevka, P.2    Kuhn, R.J.3    Rossmann, M.G.4
  • 49
    • 33751225391 scopus 로고    scopus 로고
    • Transmission electron microtomography without the "missing wedge" for quantitative structural analysis
    • DOI 10.1016/j.ultramic.2006.04.007, PII S0304399106000775
    • N. Kawase, M. Kato, H. Nishioka, and H. Jinnai Transmission electron microtomography without the "missing wedge" for quantitative structural analysis Ultramicroscopy 107 2007 8 15 (Pubitemid 44792866)
    • (2007) Ultramicroscopy , vol.107 , Issue.1 , pp. 8-15
    • Kawase, N.1    Kato, M.2    Nishioka, H.3    Jinnai, H.4
  • 50
  • 53
    • 0029644940 scopus 로고
    • Where freedom is given, liberties are taken
    • G.J. Kleywegt, and T.A. Jones Where freedom is given, liberties are taken Structure 3 1995 535 540
    • (1995) Structure , vol.3 , pp. 535-540
    • Kleywegt, G.J.1    Jones, T.A.2
  • 54
    • 0026566946 scopus 로고
    • Automated microscopy for electron tomography
    • A.J. Koster, H. Chen, J.W. Sedat, and D.A. Agard Automated microscopy for electron tomography Ultramicroscopy 46 1992 207 227 (Pubitemid 23600805)
    • (1992) Ultramicroscopy , vol.45 , Issue.1-4 , pp. 207-227
    • Koster, A.J.1    Chen, H.2    Sedat, J.W.3    Agard, D.A.4
  • 57
    • 77956098333 scopus 로고    scopus 로고
    • Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks
    • H. Liu, L. Jin, S.B.S. Koh, I. Atanasov, S. Schein, and L. Wu Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks Science 329 2010 1038 1043
    • (2010) Science , vol.329 , pp. 1038-1043
    • Liu, H.1    Jin, L.2    Koh, S.B.S.3    Atanasov, I.4    Schein, S.5    Wu, L.6
  • 58
    • 77954384340 scopus 로고    scopus 로고
    • Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus
    • X. Liu, Q. Zhang, K. Murata, M.L. Baker, M.B. Sullivan, and C. Fu Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus Nat. Struct. Mol. Biol. 17 2010 830 836
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 830-836
    • Liu, X.1    Zhang, Q.2    Murata, K.3    Baker, M.L.4    Sullivan, M.B.5    Fu, C.6
  • 59
    • 67749131110 scopus 로고    scopus 로고
    • Paramyxovirus ultrastructure and genome packaging: Cryo-electron tomography of sendai virus
    • C. Loney, G. Mottet-Osman, L. Roux, and D. Bhella Paramyxovirus ultrastructure and genome packaging: cryo-electron tomography of sendai virus J. Virol. 83 2009 8191 8197
    • (2009) J. Virol. , vol.83 , pp. 8191-8197
    • Loney, C.1    Mottet-Osman, G.2    Roux, L.3    Bhella, D.4
  • 60
    • 51149201181 scopus 로고
    • The structure of the benzene ring
    • K. Lonsdale The structure of the benzene ring Nature 122 1928 810
    • (1928) Nature , vol.122 , pp. 810
    • Lonsdale, K.1
  • 61
    • 14844330221 scopus 로고    scopus 로고
    • Structural studies by electron tomography: From cells to molecules
    • DOI 10.1146/annurev.biochem.73.011303.074112
    • V. Lui, F. Frster, and W. Baumeister Structural studies by electron tomography: from cells to molecules Ann. Rev. Biochem. 74 2005 833 865 (Pubitemid 40995525)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 833-865
    • Lucic, V.1    Forster, F.2    Baumeister, W.3
  • 62
    • 0037044862 scopus 로고    scopus 로고
    • Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography
    • DOI 10.1126/science.1076184
    • O. Medalia, I. Weber, A.S. Frangakis, D. Nicastro, G. Gerisch, and W. Baumeister Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography Science 298 2002 1209 1213 (Pubitemid 35285482)
    • (2002) Science , vol.298 , Issue.5596 , pp. 1209-1213
    • Medalia, O.1    Weber, I.2    Frangakis, A.S.3    Nicastro, D.4    Gerisch, G.5    Baumeister, W.6
  • 63
    • 77953538191 scopus 로고    scopus 로고
    • Characterization of a direct detection device imaging camera for transmission electron microscopy
    • A.-C. Milazzo, G. Moldovan, J. Lanman, L. Jin, J.C. Bouwer, and S. Klienfelder Characterization of a direct detection device imaging camera for transmission electron microscopy Ultramicroscopy 110 2010 744 747
    • (2010) Ultramicroscopy , vol.110 , pp. 744-747
    • Milazzo, A.-C.1    Moldovan, G.2    Lanman, J.3    Jin, L.4    Bouwer, J.C.5    Klienfelder, S.6
  • 64
    • 77955481741 scopus 로고    scopus 로고
    • Zernike phase contrast cryo-electron microscopy and tomography for structure determination at nanometer and subnanometer resolutions
    • K. Murata, X. Liu, R. Danev, J. Jakana, M.F. Schmid, and J. King Zernike phase contrast cryo-electron microscopy and tomography for structure determination at nanometer and subnanometer resolutions Structure 18 2010 903 912
    • (2010) Structure , vol.18 , pp. 903-912
    • Murata, K.1    Liu, X.2    Danev, R.3    Jakana, J.4    Schmid, M.F.5    King, J.6
  • 66
    • 33750527990 scopus 로고    scopus 로고
    • Mapping 70S ribosomes in intact cells by cryoelectron tomography and pattern recognition
    • DOI 10.1016/j.jsb.2006.04.014, PII S1047847706001638
    • J.O. Ortiz, F. Frster, J. Krner, A.A. Linaroudis, and W. Baumeister Mapping 70S ribosomes in intact cells by cryoelectron tomography and pattern recognition J. Struct. Biol. 156 2006 334 341 (Pubitemid 44666445)
    • (2006) Journal of Structural Biology , vol.156 , Issue.2 , pp. 334-341
    • Ortiz, J.O.1    Forster, F.2    Kurner, J.3    Linaroudis, A.A.4    Baumeister, W.5
  • 68
    • 0000070408 scopus 로고
    • A Fourier series method for the determination of the components of interatomic distances in crystals
    • A.L. Patterson A Fourier series method for the determination of the components of interatomic distances in crystals Phys. Rev. 46 1934 372 376
    • (1934) Phys. Rev. , vol.46 , pp. 372-376
    • Patterson, A.L.1
  • 69
    • 0001598843 scopus 로고
    • A direct method for the determination of the components of interatomic distances in crystals
    • A.L. Patterson A direct method for the determination of the components of interatomic distances in crystals Z. Kristallogr. 90 1935 517 542
    • (1935) Z. Kristallogr. , vol.90 , pp. 517-542
    • Patterson, A.L.1
  • 70
    • 36949066642 scopus 로고
    • Structure of haemoglobin. A three-dimensional Fourier synthesis at 5.5- resolution, obtained by X-ray analysis
    • M.F. Perutz, M.G. Rossmann, A.F. Cullis, H. Muirhead, G. Will, and A.C.T. North Structure of haemoglobin. A three-dimensional Fourier synthesis at 5.5- resolution, obtained by X-ray analysis Nature 185 1960 416 422
    • (1960) Nature , vol.185 , pp. 416-422
    • Perutz, M.F.1    Rossmann, M.G.2    Cullis, A.F.3    Muirhead, H.4    Will, G.5    North, A.C.T.6
  • 71
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • DOI 10.1016/j.jmb.2003.07.013
    • 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 (Pubitemid 37268015)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.4 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 72
    • 0033780164 scopus 로고    scopus 로고
    • Fitting atomic models into electron microscopy maps
    • M.G. Rossmann Fitting atomic models into electron microscopy maps Acta Crystallogr. D Biol. Crystallogr. 56 2000 1341 1349
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1341-1349
    • Rossmann, M.G.1
  • 74
    • 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, and H.J. Hecht 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
  • 75
    • 0035783056 scopus 로고    scopus 로고
    • Combining electron microscopic with X-ray crystallographic structures
    • M.G. Rossmann, R. Bernal, and S.V. Pletnev Combining electron microscopic with X-ray crystallographic structures J. Struct. Biol. 136 2001 190 200
    • (2001) J. Struct. Biol. , vol.136 , pp. 190-200
    • Rossmann, M.G.1    Bernal, R.2    Pletnev, S.V.3
  • 77
    • 33845939047 scopus 로고    scopus 로고
    • Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization
    • DOI 10.1038/nmeth992, PII NMETH992
    • S.H.W. Scheres, H. Gao, M. Valle, G.T. Herman, P.P.B. Eggermont, and J. Frank Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization Nat. Methods 4 2007 27 29 (Pubitemid 46029470)
    • (2007) Nature Methods , vol.4 , Issue.1 , pp. 27-29
    • Scheres, S.H.W.1    Gao, H.2    Valle, M.3    Herman, G.T.4    Eggermont, P.P.B.5    Frank, J.6    Carazo, J.-M.7
  • 81
    • 0031058884 scopus 로고    scopus 로고
    • Rotation function calculations with GLRF program
    • DOI 10.1016/S0076-6879(97)76080-4
    • L. Tong, and M.G. Rossmann Rotation function calculations with GLRF program Methods Enzymol. 276 1997 594 611 (Pubitemid 27085625)
    • (1997) Methods in Enzymology , vol.276 , pp. 594-611
    • Tong, L.1    Rossmann, M.G.2
  • 82
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • P.N.T. Unwin, and R. Henderson Molecular structure determination by electron microscopy of unstained crystalline specimens J. Mol. Biol. 94 1975 425 440
    • (1975) J. Mol. Biol. , vol.94 , pp. 425-440
    • Unwin, P.N.T.1    Henderson, R.2
  • 83
    • 25144494651 scopus 로고    scopus 로고
    • Fourier shell correlation threshold criteria
    • DOI 10.1016/j.jsb.2005.05.009, PII S1047847705001292
    • M. van Heel, and M. Schatz Fourier shell correlation threshold criteria J. Struct. Biol. 151 2005 250 262 (Pubitemid 41338732)
    • (2005) Journal of Structural Biology , vol.151 , Issue.3 , pp. 250-262
    • Van Heel, M.1    Schatz, M.2
  • 84
    • 68149170539 scopus 로고    scopus 로고
    • Confidence intervals for fitting of atomic models into low-resolution densities
    • N. Volkmann Confidence intervals for fitting of atomic models into low-resolution densities Acta Crystallogr. D Biol. Crystallogr. 65 2009 679 689
    • (2009) Acta Crystallogr. D Biol. Crystallogr. , vol.65 , pp. 679-689
    • Volkmann, N.1
  • 85
    • 0347380212 scopus 로고    scopus 로고
    • Docking of Atomic Models into Reconstructions from Electron Microscopy
    • DOI 10.1016/S0076-6879(03)74010-5
    • N. Volkmann, and D. Hanein Docking of atomic models into reconstructions from electron microscopy Methods Enzymol. 374 2003 204 225 (Pubitemid 37547910)
    • (2003) Methods in Enzymology , vol.374 , pp. 204-225
    • Volkmann, N.1    Hanein, D.2
  • 86
    • 0028773903 scopus 로고
    • The structure of a neutralized virus: Canine parvovirus complexed with neutralizing antibody fragment
    • W.R. Wikoff, G. Wang, C.R. Parrish, R.H. Cheng, M.L. Strassheim, and T.S. Baker The structure of a neutralized virus: canine parvovirus complexed with neutralizing antibody fragment Structure 2 1994 595 607
    • (1994) Structure , vol.2 , pp. 595-607
    • Wikoff, W.R.1    Wang, G.2    Parrish, C.R.3    Cheng, R.H.4    Strassheim, M.L.5    Baker, T.S.6
  • 87
    • 43749092377 scopus 로고    scopus 로고
    • 3.88 A structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy
    • DOI 10.1038/nature06893, PII NATURE06893
    • X. Yu, L. Jin, and Z.H. Zhou 3.88 structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy Nature 453 2008 415 419 (Pubitemid 351693126)
    • (2008) Nature , vol.453 , Issue.7193 , pp. 415-419
    • Yu, X.1    Jin, L.2    Zhou, Z.H.3
  • 88
    • 33748038359 scopus 로고    scopus 로고
    • Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ
    • G. Zanetti, J.A. Briggs, K. Grnewald, Q.J. Sattentau, and S.D. Fuller Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ PLoS Pathog. 2 8 2006 e83
    • (2006) PLoS Pathog. , vol.2 , Issue.8 , pp. 83
    • Zanetti, G.1    Briggs, J.A.2    Grnewald, K.3    Sattentau, Q.J.4    Fuller, S.D.5
  • 89
    • 77951912692 scopus 로고    scopus 로고
    • 3.3 cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry
    • X. Zhang, L. Jin, Q. Fang, W.H. Hui, and Z.H. Zhou 3.3 cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry Cell 141 2010 472 482
    • (2010) Cell , vol.141 , pp. 472-482
    • Zhang, X.1    Jin, L.2    Fang, Q.3    Hui, W.H.4    Zhou, Z.H.5
  • 91
    • 33745203490 scopus 로고    scopus 로고
    • Distribution and three-dimensional structure of AIDS virus envelope spikes
    • P. Zhu, J. Liu, J. Bess Jr., E. Chertova, J.D. Lifson, and H. Gris Distribution and three-dimensional structure of AIDS virus envelope spikes Nature 441 2006 847 852
    • (2006) Nature , vol.441 , pp. 847-852
    • Zhu, P.1    Liu, J.2    Bess Jr., J.3    Chertova, E.4    Lifson, J.D.5    Gris, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.