메뉴 건너뛰기




Volumn 1, Issue , 2012, Pages 311-340

Cryo-electron microscopy and tomography of virus particles

Author keywords

Cryo EM; Cryo ET; Molecular biology; Virus reconstruction; Virus structure

Indexed keywords


EID: 84863023972     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374920-8.00120-X     Document Type: Chapter
Times cited : (4)

References (103)
  • 1
    • 0014930077 scopus 로고
    • Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther R., Amos L., Finch J., De Rosier D., Klug A. Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs. Nature 1970, 226:421-425.
    • (1970) Nature , vol.226 , pp. 421-425
    • Crowther, R.1    Amos, L.2    Finch, J.3    De Rosier, D.4    Klug, A.5
  • 2
    • 0000668797 scopus 로고
    • Reconstruction of three-dimensional structures from electron micrographs
    • DeRosier D.A., Klug A. Reconstruction of three-dimensional structures from electron micrographs. Nature 1968, 217:130-134.
    • (1968) Nature , vol.217 , pp. 130-134
    • DeRosier, D.A.1    Klug, A.2
  • 4
    • 39849102970 scopus 로고    scopus 로고
    • Backbone structure of the infectious epsilon15 virus capsid revealed by electron cryomicroscopy
    • Jiang W., Baker M., Jakana J., Weigele P., King J., Chiu W. Backbone structure of the infectious epsilon15 virus capsid revealed by electron cryomicroscopy. Nature 2008, 451:1130-1134.
    • (2008) Nature , vol.451 , pp. 1130-1134
    • Jiang, W.1    Baker, M.2    Jakana, J.3    Weigele, P.4    King, J.5    Chiu, W.6
  • 5
    • 77956098333 scopus 로고    scopus 로고
    • Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks
    • Liu H., Jin L., Koh S.B.S., Atanasov I., Schein S., Wu L., Zhou Z.H. Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks. Science 2010, 329:1038-1043.
    • (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    Zhou, Z.H.7
  • 7
    • 34447649588 scopus 로고    scopus 로고
    • High-resolution electron microscopy of helical specimens: A fresh look at tobacco mosaic virus
    • Sachse C., Chen J., Coureux P.-D., Stroupe M., Fändrich M., Grigorieff N. High-resolution electron microscopy of helical specimens: A fresh look at tobacco mosaic virus. J. Mol. Biol. 2007, 371:812-835.
    • (2007) J. Mol. Biol. , vol.371 , pp. 812-835
    • Sachse, C.1    Chen, J.2    Coureux, P.-D.3    Stroupe, M.4    Fändrich, M.5    Grigorieff, N.6
  • 9
    • 43749092377 scopus 로고    scopus 로고
    • 3.88 A structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy
    • Yu X., Jin L., Zhou Z. 3.88 A structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy. Nature 2008, 453:415-419.
    • (2008) Nature , vol.453 , pp. 415-419
    • Yu, X.1    Jin, L.2    Zhou, Z.3
  • 10
    • 77951912692 scopus 로고    scopus 로고
    • 3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry
    • Zhang X., Jin L., Fang Q., Hui W.H., Zhou Z.H. 3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry. Cell 2010, 141:472-482.
    • (2010) Cell , vol.141 , pp. 472-482
    • Zhang, X.1    Jin, L.2    Fang, Q.3    Hui, W.H.4    Zhou, Z.H.5
  • 12
  • 13
    • 33744811672 scopus 로고    scopus 로고
    • Cryo-EM asymmetric reconstruction of bacteriophage P22 reveals organization of its DNA packaging and infecting machinery
    • Chang J., Weigele P., King J., Chiu W., Jiang W. Cryo-EM asymmetric reconstruction of bacteriophage P22 reveals organization of its DNA packaging and infecting machinery. Structure 2006, 14:1073-1082.
    • (2006) Structure , vol.14 , pp. 1073-1082
    • Chang, J.1    Weigele, P.2    King, J.3    Chiu, W.4    Jiang, W.5
  • 14
    • 31844435708 scopus 로고    scopus 로고
    • Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus
    • Jiang W., Chang J., Jakana J., Weigele P., King J., Chiu W. Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus. Nature 2006, 439:612-616.
    • (2006) Nature , vol.439 , pp. 612-616
    • Jiang, W.1    Chang, J.2    Jakana, J.3    Weigele, P.4    King, J.5    Chiu, W.6
  • 16
    • 77955481741 scopus 로고    scopus 로고
    • Zernike phase contrast cryo-electron microscopy and tomography for structure determination at nanometer and subnanometer resolutions
    • Murata K., Liu X., Danev R., Jakana J., Schmid M.F., King J., Nagayama K., Chiu W. Zernike phase contrast cryo-electron microscopy and tomography for structure determination at nanometer and subnanometer resolutions. Structure 2010, 18:903-912.
    • (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    Nagayama, K.7    Chiu, W.8
  • 18
    • 0032712359 scopus 로고    scopus 로고
    • Adding the third dimension to virus life cycles: Three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs
    • Baker T.S., Olson N.H., Fuller S.D. Adding the third dimension to virus life cycles: Three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs. Microbiol. Mol. Biol. Rev. 1999, 63:862-922.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 862-922
    • Baker, T.S.1    Olson, N.H.2    Fuller, S.D.3
  • 19
    • 34548008824 scopus 로고    scopus 로고
    • Cryoelectron microscopy of icosahedral virus particles
    • Jiang W., Chiu W. Cryoelectron microscopy of icosahedral virus particles. Methods Mol. Biol. 2007, 369:345-363.
    • (2007) Methods Mol. Biol. , vol.369 , pp. 345-363
    • Jiang, W.1    Chiu, W.2
  • 20
    • 0034044540 scopus 로고    scopus 로고
    • Reconstruction principles of icosahedral virus structure determination using electron cryomicroscopy
    • Thuman-Commike P., Chiu W. Reconstruction principles of icosahedral virus structure determination using electron cryomicroscopy. Micron 2000, 31:687-711.
    • (2000) Micron , vol.31 , pp. 687-711
    • Thuman-Commike, P.1    Chiu, W.2
  • 21
    • 0042827239 scopus 로고    scopus 로고
    • Determination of icosahedral virus structures by electron cryomicroscopy at subnanometer resolution
    • Zhou Z., Chiu W. Determination of icosahedral virus structures by electron cryomicroscopy at subnanometer resolution. Adv. Protein Chem 2003, 64:93-124.
    • (2003) Adv. Protein Chem , vol.64 , pp. 93-124
    • Zhou, Z.1    Chiu, W.2
  • 22
    • 0015242161 scopus 로고
    • Three-dimensional reconstruction of the stacked-disk aggregate of tobacco mosaic virus protein from electron micrographs
    • Finch J.T., Klug A. Three-dimensional reconstruction of the stacked-disk aggregate of tobacco mosaic virus protein from electron micrographs. Philos. Trans. R. Soc. London B Biol. Sci 1971, 261:211-219.
    • (1971) Philos. Trans. R. Soc. London B Biol. Sci , vol.261 , pp. 211-219
    • Finch, J.T.1    Klug, A.2
  • 23
  • 25
    • 16344390563 scopus 로고    scopus 로고
    • Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography
    • Förster F., Medalia O., Zauberman N., Baumeister W., Fass D. Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography. Proc. Natl. Acad. Sci. USA 2005, 102:4729-4734.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4729-4734
    • Förster, F.1    Medalia, O.2    Zauberman, N.3    Baumeister, W.4    Fass, D.5
  • 27
    • 33846785568 scopus 로고    scopus 로고
    • Electron cryotomography reveals the portal in the herpesvirus capsid
    • Chang J., Schmid M., Rixon F., Chiu W. Electron cryotomography reveals the portal in the herpesvirus capsid. J. Virol. 2007, 81:2065-2068.
    • (2007) J. Virol. , vol.81 , pp. 2065-2068
    • Chang, J.1    Schmid, M.2    Rixon, F.3    Chiu, W.4
  • 28
    • 40649109028 scopus 로고    scopus 로고
    • Methods for aligning and for averaging 3D volumes with missing data
    • Schmid M., Booth C. Methods for aligning and for averaging 3D volumes with missing data. J. Struct. Biol. 2008, 161:243-248.
    • (2008) J. Struct. Biol. , vol.161 , pp. 243-248
    • Schmid, M.1    Booth, C.2
  • 30
    • 76749094569 scopus 로고    scopus 로고
    • The resolution dependence of optimal exposures in liquid nitrogen temperature electron cryomicroscopy of catalase crystals
    • Baker L.A., Smith E.A., Bueler S.A., Rubinstein J.L. The resolution dependence of optimal exposures in liquid nitrogen temperature electron cryomicroscopy of catalase crystals. J. Struct. Biol. 2010, 169:431-437.
    • (2010) J. Struct. Biol. , vol.169 , pp. 431-437
    • Baker, L.A.1    Smith, E.A.2    Bueler, S.A.3    Rubinstein, J.L.4
  • 31
    • 76749153367 scopus 로고    scopus 로고
    • Radiation damage effects at four specimen temperatures from 4 to 100 K
    • Bammes B.E., Jakana J., Schmid M.F., Chiu W. Radiation damage effects at four specimen temperatures from 4 to 100 K. J. Struct. Biol. 2010, 169:331-341.
    • (2010) J. Struct. Biol. , vol.169 , pp. 331-341
    • Bammes, B.E.1    Jakana, J.2    Schmid, M.F.3    Chiu, W.4
  • 32
    • 0029379689 scopus 로고
    • The relevance of dose-fractionation in tomography of radiation-sensitive specimens
    • McEwen B.F., Downing K.H., Glaeser R.M. The relevance of dose-fractionation in tomography of radiation-sensitive specimens. Ultramicroscopy 1995, 60:357-373.
    • (1995) Ultramicroscopy , vol.60 , pp. 357-373
    • McEwen, B.F.1    Downing, K.H.2    Glaeser, R.M.3
  • 36
    • 0023317718 scopus 로고
    • Is Sindbis a simple picornavirus with an envelope?
    • Fuller S.D., Argos P. Is Sindbis a simple picornavirus with an envelope?. EMBO J. 1987, 6:1099-1105.
    • (1987) EMBO J. , vol.6 , pp. 1099-1105
    • Fuller, S.D.1    Argos, P.2
  • 38
    • 0037313264 scopus 로고    scopus 로고
    • Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions
    • Jiang W., Li Z., Zhang Z., Baker M., Prevelige P., Chiu W. Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Nature Struct. Biol. 2003, 10:131-135.
    • (2003) Nature Struct. Biol. , vol.10 , pp. 131-135
    • Jiang, W.1    Li, Z.2    Zhang, Z.3    Baker, M.4    Prevelige, P.5    Chiu, W.6
  • 39
    • 0022734165 scopus 로고
    • High-resolution imaging magnetic energy filters with simple structure
    • Lanio S. High-resolution imaging magnetic energy filters with simple structure. OPTIK 1986, 73:99-107.
    • (1986) OPTIK , vol.73 , pp. 99-107
    • Lanio, S.1
  • 40
    • 0032423352 scopus 로고    scopus 로고
    • Non-isochromaticity of an omega filter in a 200 kV transmission electron microscope
    • Tsuno K., Kaneyama T., Honda T., Ishida Y. Non-isochromaticity of an omega filter in a 200 kV transmission electron microscope. J. Electron Microsc. 1998, 47:611-619.
    • (1998) J. Electron Microsc. , vol.47 , pp. 611-619
    • Tsuno, K.1    Kaneyama, T.2    Honda, T.3    Ishida, Y.4
  • 42
    • 45549095742 scopus 로고    scopus 로고
    • Achievable resolution from images of biological specimens acquired from a 4k×4k CCD camera in a 300-kV electron cryomicroscope
    • Chen D.-H., Jakana J., Liu X., Schmid M., Chiu W. Achievable resolution from images of biological specimens acquired from a 4k×4k CCD camera in a 300-kV electron cryomicroscope. J. Struct. Biol. 2008, 163:45-52.
    • (2008) J. Struct. Biol. , vol.163 , pp. 45-52
    • Chen, D.-H.1    Jakana, J.2    Liu, X.3    Schmid, M.4    Chiu, W.5
  • 44
    • 33750997853 scopus 로고    scopus 로고
    • Assessing the capabilities of a 4k×4k CCD camera for electron cryo-microscopy at 300kV
    • Booth C., Jakana J., Chiu W. Assessing the capabilities of a 4k×4k CCD camera for electron cryo-microscopy at 300kV. J. Struct. Biol 2006, 156:556-563.
    • (2006) J. Struct. Biol , vol.156 , pp. 556-563
    • Booth, C.1    Jakana, J.2    Chiu, W.3
  • 45
    • 0028569793 scopus 로고
    • Applications of a slow-scan CCD camera in protein electron crystallography
    • Brink J., Chiu W. Applications of a slow-scan CCD camera in protein electron crystallography. J. Struct. Biol. 1994, 113:23-34.
    • (1994) J. Struct. Biol. , vol.113 , pp. 23-34
    • Brink, J.1    Chiu, W.2
  • 46
    • 0030114748 scopus 로고    scopus 로고
    • Performance of a slow-scan CCD camera for macromolecular imaging in a 400 kV electron cryomicroscope
    • Sherman M.B., Brink J., Chiu W. Performance of a slow-scan CCD camera for macromolecular imaging in a 400 kV electron cryomicroscope. Micron 1996, 27:129-139.
    • (1996) Micron , vol.27 , pp. 129-139
    • Sherman, M.B.1    Brink, J.2    Chiu, W.3
  • 47
    • 0033774875 scopus 로고    scopus 로고
    • Digital imaging in transmission electron microscopy
    • Fan G., Ellisman M. Digital imaging in transmission electron microscopy. J. Microsc. 2000, 200:1-13.
    • (2000) J. Microsc. , vol.200 , pp. 1-13
    • Fan, G.1    Ellisman, M.2
  • 48
    • 16644365074 scopus 로고    scopus 로고
    • 9 angstroms single particle reconstruction from CCD captured images on a 200kV electron cryomicroscope
    • Booth C., Jiang W., Baker M., Zhou Z., Ludtke S., Chiu W.A 9 angstroms single particle reconstruction from CCD captured images on a 200kV electron cryomicroscope. J. Struct. Biol. 2004, 147:116-127.
    • (2004) J. Struct. Biol. , vol.147 , pp. 116-127
    • Booth, C.1    Jiang, W.2    Baker, M.3    Zhou, Z.4    Ludtke, S.5    Chiu, W.A.6
  • 50
    • 0942299966 scopus 로고    scopus 로고
    • Object oriented database and electronic notebook for transmission electron microscopy
    • Ludtke S., Nason L., Tu H., Peng L., Chiu W. Object oriented database and electronic notebook for transmission electron microscopy. Microsc. Microanal. 2003, 9:556-565.
    • (2003) Microsc. Microanal. , vol.9 , pp. 556-565
    • Ludtke, S.1    Nason, L.2    Tu, H.3    Peng, L.4    Chiu, W.5
  • 51
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S., Baldwin P., Chiu W. EMAN: Semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 1999, 128:82-97.
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.1    Baldwin, P.2    Chiu, W.3
  • 54
    • 0000186608 scopus 로고
    • Measurement and compensation of de-focusing and aberrations by Fourier processing of electron micrographs
    • Erickson H., Klug A. Measurement and compensation of de-focusing and aberrations by Fourier processing of electron micrographs. Philos. Trans. R. Soc. London B 1971, 261:105-118.
    • (1971) Philos. Trans. R. Soc. London B , vol.261 , pp. 105-118
    • Erickson, H.1    Klug, A.2
  • 55
    • 0002228874 scopus 로고
    • Phase Contrast Electron Microscopy.
    • Academic Press: London
    • Thon, F. Phase Contrast Electron Microscopy. In Electron Microscopy in Material Sciences; Academic Press: London, 1971; pp. 571-625.
    • (1971) In Electron Microscopy in Material Sciences , pp. 571-625
    • Thon, F.1
  • 56
    • 0035782663 scopus 로고    scopus 로고
    • Fourier amplitude decay of electron cryomicroscopic images of single particles and effects on structure determination
    • Saad A., Ludtke S., Jakana J., Rixon F., Tsuruta H., Chiu W. Fourier amplitude decay of electron cryomicroscopic images of single particles and effects on structure determination. J. Struct. Biol. 2001, 133:32-42.
    • (2001) J. Struct. Biol. , vol.133 , pp. 32-42
    • Saad, A.1    Ludtke, S.2    Jakana, J.3    Rixon, F.4    Tsuruta, H.5    Chiu, W.6
  • 57
    • 66149086013 scopus 로고    scopus 로고
    • The putative leucine zipper of the UL6-encoded portal protein of herpes simplex virus 1 is necessary for interaction with pUL15 and pUL28 and their association with capsids
    • Yang K., Wills E., Baines J. The putative leucine zipper of the UL6-encoded portal protein of herpes simplex virus 1 is necessary for interaction with pUL15 and pUL28 and their association with capsids. J. Virol. 2009, 83:4557-4564.
    • (2009) J. Virol. , vol.83 , pp. 4557-4564
    • Yang, K.1    Wills, E.2    Baines, J.3
  • 58
    • 34548643898 scopus 로고    scopus 로고
    • Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm
    • Liu X., Jiang W., Jakana J., Chiu W. Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. J. Struct. Biol. 2007, 160:11-27.
    • (2007) J. Struct. Biol. , vol.160 , pp. 11-27
    • Liu, X.1    Jiang, W.2    Jakana, J.3    Chiu, W.4
  • 60
    • 0032582665 scopus 로고    scopus 로고
    • Assembly of a tailed bacterial virus and its genome release studied in three dimensions
    • Tao Y., Olson N.H., Xu W., Anderson D.L., Rossmann M.G., Baker T.S. Assembly of a tailed bacterial virus and its genome release studied in three dimensions. Cell 1998, 95:431-437.
    • (1998) Cell , vol.95 , pp. 431-437
    • Tao, Y.1    Olson, N.H.2    Xu, W.3    Anderson, D.L.4    Rossmann, M.G.5    Baker, T.S.6
  • 61
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER 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 WEB Processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 1996, 116:190-199.
    • (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
  • 64
    • 8844219659 scopus 로고    scopus 로고
    • Noise bias in the refinement of structures derived from single particles
    • Stewart A., Grigorieff N. Noise bias in the refinement of structures derived from single particles. Ultramicroscopy 2004, 102:67-84.
    • (2004) Ultramicroscopy , vol.102 , pp. 67-84
    • Stewart, A.1    Grigorieff, N.2
  • 65
    • 33845338800 scopus 로고    scopus 로고
    • AUTO3DEM: An automated and high throughput program for image reconstruction of icosahedral particles
    • Yan X., Sinkovits R., Baker T. AUTO3DEM: An automated and high throughput program for image reconstruction of icosahedral particles. J. Struct. Biol. 2007, 157:73-82.
    • (2007) J. Struct. Biol. , vol.157 , pp. 73-82
    • Yan, X.1    Sinkovits, R.2    Baker, T.3
  • 67
    • 0036420061 scopus 로고    scopus 로고
    • IMIRS: A high-resolution 3D reconstruction package integrated with a relational image database
    • Liang Y., Ke E., Zhou Z. IMIRS: A high-resolution 3D reconstruction package integrated with a relational image database. J. Struct. Biol. 2002, 137:292-304.
    • (2002) J. Struct. Biol. , vol.137 , pp. 292-304
    • Liang, Y.1    Ke, E.2    Zhou, Z.3
  • 68
    • 0029924120 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of icosahedral particles: The uncommon line
    • Fuller S., Butcher S., Cheng R., Baker T. Three-dimensional reconstruction of icosahedral particles: The uncommon line. J. Struct. Biol. 1996, 116:48-55.
    • (1996) J. Struct. Biol. , vol.116 , pp. 48-55
    • Fuller, S.1    Butcher, S.2    Cheng, R.3    Baker, T.4
  • 70
    • 77649128082 scopus 로고    scopus 로고
    • P22 coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical crosslinks
    • Parent K.N., Khayat R., Tu L.H., Suhanovsky M.M., Cortines J.R., Teschke C.M., Johnson J.E., Baker T.S. P22 coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical crosslinks. Structure 2010, 18:390-401.
    • (2010) Structure , vol.18 , pp. 390-401
    • Parent, K.N.1    Khayat, R.2    Tu, L.H.3    Suhanovsky, M.M.4    Cortines, J.R.5    Teschke, C.M.6    Johnson, J.E.7    Baker, T.S.8
  • 71
    • 0033377941 scopus 로고    scopus 로고
    • Electron crystallography: Present excitement, a nod to the past, anticipating the future
    • Glaeser R. Electron crystallography: Present excitement, a nod to the past, anticipating the future. J. Struct. Biol. 1999, 128:3-14.
    • (1999) J. Struct. Biol. , vol.128 , pp. 3-14
    • Glaeser, R.1
  • 72
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal P., Henderson R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 2003, 333:721-745.
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.1    Henderson, R.2
  • 73
    • 0032540273 scopus 로고    scopus 로고
    • Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 A in ice
    • Grigorieff N. Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 A in ice. J. Mol. Biol. 1998, 277:1033-1046.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1033-1046
    • Grigorieff, N.1
  • 74
    • 14844330221 scopus 로고    scopus 로고
    • Structural studies by electron tomography: From cells to molecules
    • Lucić V., Förster F., Baumeister W. Structural studies by electron tomography: From cells to molecules. Annu. Rev. Biochem. 2005, 74:833-865.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 833-865
    • Lucić, V.1    Förster, F.2    Baumeister, W.3
  • 75
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer J., Mastronarde D., McIntosh J. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 1996, 116:71-76.
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.1    Mastronarde, D.2    McIntosh, J.3
  • 76
  • 77
    • 33846061281 scopus 로고    scopus 로고
    • Identification of secondary structure elements in intermediate-resolution density maps
    • Baker M., Ju T., Chiu W. Identification of secondary structure elements in intermediate-resolution density maps. Structure 2007, 15:7-19.
    • (2007) Structure , vol.15 , pp. 7-19
    • Baker, M.1    Ju, T.2    Chiu, W.3
  • 80
    • 0000313739 scopus 로고
    • Exact filters for general geometry three dimensional reconstruction
    • Harauz G., Van Heel M. Exact filters for general geometry three dimensional reconstruction. OPTIK 1986, 73:146-156.
    • (1986) OPTIK , vol.73 , pp. 146-156
    • Harauz, G.1    Van Heel, M.2
  • 81
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial cell envelope protein
    • Saxton W., Baumeister W. The correlation averaging of a regularly arranged bacterial cell envelope protein. J. Microsc. 1982, 127:127-138.
    • (1982) J. Microsc. , vol.127 , pp. 127-138
    • Saxton, W.1    Baumeister, W.2
  • 82
    • 77954643550 scopus 로고    scopus 로고
    • Definition and estimation of resolution in single-particle reconstructions
    • Liao H.Y., Frank J. Definition and estimation of resolution in single-particle reconstructions. Structure 2010, 18:768-775.
    • (2010) Structure , vol.18 , pp. 768-775
    • Liao, H.Y.1    Frank, J.2
  • 83
    • 25144494651 scopus 로고    scopus 로고
    • Fourier shell correlation threshold criteria
    • van Heel M., Schatz M. Fourier shell correlation threshold criteria. J. Struct. Biol. 2005, 151:250-262.
    • (2005) J. Struct. Biol. , vol.151 , pp. 250-262
    • van Heel, M.1    Schatz, M.2
  • 84
    • 0029991985 scopus 로고    scopus 로고
    • A flexible environment for the visualization of three-dimensional biological structures
    • Hessler D., Young S., Ellisman M. A flexible environment for the visualization of three-dimensional biological structures. J. Struct. Biol. 1996, 116:113-119.
    • (1996) J. Struct. Biol. , vol.116 , pp. 113-119
    • Hessler, D.1    Young, S.2    Ellisman, M.3
  • 85
    • 0031405779 scopus 로고    scopus 로고
    • Tinkerbell: A tool for interactive segmentation of 3D data
    • Li Y., Leith A., Frank J. Tinkerbell: A tool for interactive segmentation of 3D data. J. Struct. Biol. 1997, 120:266-275.
    • (1997) J. Struct. Biol. , vol.120 , pp. 266-275
    • Li, Y.1    Leith, A.2    Frank, J.3
  • 86
    • 0036424944 scopus 로고    scopus 로고
    • A novel three-dimensional variant of the watershed transform for segmentation of electron density maps
    • Volkmann N. A novel three-dimensional variant of the watershed transform for segmentation of electron density maps. J. Struct. Biol 2002, 138:123-129.
    • (2002) J. Struct. Biol , vol.138 , pp. 123-129
    • Volkmann, N.1
  • 87
    • 0036417303 scopus 로고    scopus 로고
    • Segmentation of two- and three-dimensional data from electron microscopy using eigenvector analysis
    • Frangakis A., Hegerl R. Segmentation of two- and three-dimensional data from electron microscopy using eigenvector analysis. J. Struct. Biol. 2002, 138:105-113.
    • (2002) J. Struct. Biol. , vol.138 , pp. 105-113
    • Frangakis, A.1    Hegerl, R.2
  • 88
    • 77952581453 scopus 로고    scopus 로고
    • Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions
    • Pintilie G.D., Zhang J., Goddard T.D., Chiu W., Gossard D.C. Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions. J. Struct. Biol. 2010, 170:427-438.
    • (2010) J. Struct. Biol. , vol.170 , pp. 427-438
    • Pintilie, G.D.1    Zhang, J.2    Goddard, T.D.3    Chiu, W.4    Gossard, D.C.5
  • 89
    • 0035906702 scopus 로고    scopus 로고
    • Bridging the information gap: Computational tools for intermediate resolution structure interpretation
    • Jiang W., Baker M., Ludtke S., Chiu W. Bridging the information gap: Computational tools for intermediate resolution structure interpretation. J. Mol. Biol. 2001, 308:1033-1044.
    • (2001) J. Mol. Biol. , vol.308 , pp. 1033-1044
    • Jiang, W.1    Baker, M.2    Ludtke, S.3    Chiu, W.4
  • 93
    • 34147123766 scopus 로고    scopus 로고
    • DNA packaging and delivery machines in tailed bacteriophages
    • Johnson J., Chiu W. DNA packaging and delivery machines in tailed bacteriophages. Curr. Opin. Struct. Biol. 2007, 17:237-243.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 237-243
    • Johnson, J.1    Chiu, W.2
  • 95
    • 33846390605 scopus 로고    scopus 로고
    • Design of a microfabricated, two-electrode phase-contrast element suitable for electron microscopy
    • Cambie R., Downing K.H., Typke D., Glaeser R.M., Jin J. Design of a microfabricated, two-electrode phase-contrast element suitable for electron microscopy. Ultramicroscopy 2007, 107:329-339.
    • (2007) Ultramicroscopy , vol.107 , pp. 329-339
    • Cambie, R.1    Downing, K.H.2    Typke, D.3    Glaeser, R.M.4    Jin, J.5
  • 96
    • 0034903709 scopus 로고    scopus 로고
    • Transmission electron microscopy with Zernike phase plate
    • Danev R., Nagayama K. Transmission electron microscopy with Zernike phase plate. Ultramicroscopy 2001, 88:243-252.
    • (2001) Ultramicroscopy , vol.88 , pp. 243-252
    • Danev, R.1    Nagayama, K.2
  • 97
    • 38349081491 scopus 로고    scopus 로고
    • Single particle analysis based on Zernike phase contrast transmission electron microscopy
    • Danev R., Nagayama K. Single particle analysis based on Zernike phase contrast transmission electron microscopy. J. Struct. Biol. 2008, 161:211-218.
    • (2008) J. Struct. Biol. , vol.161 , pp. 211-218
    • Danev, R.1    Nagayama, K.2
  • 99
    • 77956892290 scopus 로고    scopus 로고
    • Visualizing the structural changes of bacteriophage epsilon15 and its Salmonella host during infection
    • Chang J.T., Schmid M.F., Haase-Pettingell C., Weigele P.R., King J.A., Chiu W. Visualizing the structural changes of bacteriophage epsilon15 and its Salmonella host during infection. J. Mol. Biol. 2010, 402:731-740.
    • (2010) J. Mol. Biol. , vol.402 , pp. 731-740
    • Chang, J.T.1    Schmid, M.F.2    Haase-Pettingell, C.3    Weigele, P.R.4    King, J.A.5    Chiu, W.6
  • 100
    • 0023059423 scopus 로고
    • Three-dimensional structure of the adenovirus major coat protein hexon
    • Roberts M.M., White J.L., Grutter M.G., Burnett R.M. Three-dimensional structure of the adenovirus major coat protein hexon. Science 1986, 232:1148-1151.
    • (1986) Science , vol.232 , pp. 1148-1151
    • Roberts, M.M.1    White, J.L.2    Grutter, M.G.3    Burnett, R.M.4
  • 101
    • 0042890357 scopus 로고    scopus 로고
    • Structural and phylogenetic analysis of adenovirus hexons by use of high-resolution X-ray crystallographic, molecular modeling, and sequence-based methods
    • Rux J.J., Kuser P.R., Burnett R.M. Structural and phylogenetic analysis of adenovirus hexons by use of high-resolution X-ray crystallographic, molecular modeling, and sequence-based methods. J. Virol. 2003, 77:9553-9566.
    • (2003) J. Virol. , vol.77 , pp. 9553-9566
    • Rux, J.J.1    Kuser, P.R.2    Burnett, R.M.3
  • 103
    • 59649112357 scopus 로고    scopus 로고
    • Rotavirus architecture at subnanometer resolution
    • Li Z., Baker M., Jiang W., Estes M., Prasad B. Rotavirus architecture at subnanometer resolution. J. Virol. 2009, 83:1754-1766.
    • (2009) J. Virol. , vol.83 , pp. 1754-1766
    • Li, Z.1    Baker, M.2    Jiang, W.3    Estes, M.4    Prasad, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.