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Volumn 435, Issue 1, 2013, Pages 179-186

Cryo-electron tomography of bacterial viruses

Author keywords

Bacteriophage; Cryo electron microscopy; Cryo electron tomography; Cryo EM; Cryo ET; Sub tomogram averaging

Indexed keywords

BACTERIOPHAGE; DNA MODIFICATION; ELECTRON MICROSCOPY; ELECTRON TOMOGRAPHY; IMAGE RECONSTRUCTION; MOLECULAR EVOLUTION; MOLECULAR IMAGING; NONHUMAN; OPTICAL RESOLUTION; PRIORITY JOURNAL; REVIEW; THREE DIMENSIONAL IMAGING; VIRUS ASSEMBLY; VIRUS ATTACHMENT; VIRUS CELL INTERACTION; VIRUS EXAMINATION; VIRUS GENOME; VIRUS MORPHOLOGY; VIRUS PARTICLE;

EID: 84870659071     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2012.08.022     Document Type: Review
Times cited : (14)

References (80)
  • 1
    • 15244343074 scopus 로고    scopus 로고
    • Structure of the connector of bacteriophage T7 at 8A resolution: structural homologies of a basic component of a DNA translocating machinery
    • Agirrezabala X., Martin-Benito J., Valle M., Gonzalez J.M., Valencia A., Valpuesta J.M., Carrascosa J.L. Structure of the connector of bacteriophage T7 at 8A resolution: structural homologies of a basic component of a DNA translocating machinery. J. Mol. Biol. 2005, 347:895-902.
    • (2005) J. Mol. Biol. , vol.347 , pp. 895-902
    • Agirrezabala, X.1    Martin-Benito, J.2    Valle, M.3    Gonzalez, J.M.4    Valencia, A.5    Valpuesta, J.M.6    Carrascosa, J.L.7
  • 3
    • 0023337259 scopus 로고
    • Membrane fusion in prokaryotes: bacteriophage phi 6 membrane fuses with the Pseudomonas syringae outer membrane
    • Bamford D.H., Romantschuk M., Somerharju P.J. Membrane fusion in prokaryotes: bacteriophage phi 6 membrane fuses with the Pseudomonas syringae outer membrane. EMBO J. 1987, 6:1467-1473.
    • (1987) EMBO J. , vol.6 , pp. 1467-1473
    • Bamford, D.H.1    Romantschuk, M.2    Somerharju, P.J.3
  • 4
    • 8344234966 scopus 로고    scopus 로고
    • Mapping molecular landscapes inside cells
    • Baumeister W. Mapping molecular landscapes inside cells. Biol. Chem. 2004, 385:865-872.
    • (2004) Biol. Chem. , vol.385 , pp. 865-872
    • Baumeister, W.1
  • 5
    • 14544297527 scopus 로고    scopus 로고
    • From proteomic inventory to architecture
    • Baumeister W. From proteomic inventory to architecture. FEBS Lett. 2005, 579:933-937.
    • (2005) FEBS Lett. , vol.579 , pp. 933-937
    • Baumeister, W.1
  • 6
  • 7
    • 0033578669 scopus 로고    scopus 로고
    • Viral evolution revealed by bacteriophage prd1 and human adenovirus coat protein structures
    • Benson S.D., Bamford J.K.H., Bamford D.H., Burnett R.M. Viral evolution revealed by bacteriophage prd1 and human adenovirus coat protein structures. Cell 1999, 98:825-833.
    • (1999) Cell , vol.98 , pp. 825-833
    • Benson, S.D.1    Bamford, J.K.H.2    Bamford, D.H.3    Burnett, R.M.4
  • 8
    • 0034687769 scopus 로고    scopus 로고
    • Toward detecting and identifying macromolecules in a cellular context: template matching applied to electron tomograms
    • Bohm J., Frangakis A.S., Hegerl R., Nickell S., Typke D., Baumeister W. Toward detecting and identifying macromolecules in a cellular context: template matching applied to electron tomograms. Proc. Nat. Acad. Sci. USA 2000, 97:14245-14250.
    • (2000) Proc. Nat. Acad. Sci. USA , vol.97 , pp. 14245-14250
    • Bohm, J.1    Frangakis, A.S.2    Hegerl, R.3    Nickell, S.4    Typke, D.5    Baumeister, W.6
  • 11
    • 33646835810 scopus 로고
    • A negative staining method for high resolution electron microscopy of viruses
    • Brenner S., Horne R.W. A negative staining method for high resolution electron microscopy of viruses. Biochim. Biophys. Acta 1959, 34:103-110.
    • (1959) Biochim. Biophys. Acta , vol.34 , pp. 103-110
    • Brenner, S.1    Horne, R.W.2
  • 13
    • 0030872369 scopus 로고    scopus 로고
    • Intermediates in the assembly pathway of the double-stranded RNA virus phi6
    • Butcher S.J., Dokland T., Ojala P.M., Bamford D.H., Fuller S.D. Intermediates in the assembly pathway of the double-stranded RNA virus phi6. EMBO J. 1997, 16:4477-4487.
    • (1997) EMBO J. , vol.16 , pp. 4477-4487
    • Butcher, S.J.1    Dokland, T.2    Ojala, P.M.3    Bamford, D.H.4    Fuller, S.D.5
  • 14
    • 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
  • 15
    • 33644851983 scopus 로고
    • An electron microscope study of isolated mitochondria: method and preliminary results
    • Claude A., Fullam E.F. An electron microscope study of isolated mitochondria: method and preliminary results. J. Exp. Med. 1945, 81:51-62.
    • (1945) J. Exp. Med. , vol.81 , pp. 51-62
    • Claude, A.1    Fullam, E.F.2
  • 18
    • 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
  • 22
    • 84857981961 scopus 로고    scopus 로고
    • Structural changes in Influenza virus at low pH characterized by cryo-electron tomography
    • Fontana J., Cardone G., Heymann J.B., Winkler D.C., Steven A.C. Structural changes in Influenza virus at low pH characterized by cryo-electron tomography. J. Virol. 2012, 86:2919-2929.
    • (2012) J. Virol. , vol.86 , pp. 2919-2929
    • Fontana, J.1    Cardone, G.2    Heymann, J.B.3    Winkler, D.C.4    Steven, A.C.5
  • 24
    • 80455122642 scopus 로고    scopus 로고
    • The mechanism of DNA ejection in the Bacillus anthracis spore-binding phage 8a revealed by cryo-electron tomography
    • Fu X., Walter M.H., Paredes A., Morais M.C., Liu J. The mechanism of DNA ejection in the Bacillus anthracis spore-binding phage 8a revealed by cryo-electron tomography. Virology 2011, 421:141-148.
    • (2011) Virology , vol.421 , pp. 141-148
    • Fu, X.1    Walter, M.H.2    Paredes, A.3    Morais, M.C.4    Liu, J.5
  • 25
    • 0015372442 scopus 로고
    • Iterative methods for the three-dimensional reconstruction of an object from projections
    • Gilbert P. Iterative methods for the three-dimensional reconstruction of an object from projections. J. Theor. Biol. 1972, 36:105-117.
    • (1972) J. Theor. Biol. , vol.36 , pp. 105-117
    • Gilbert, P.1
  • 26
    • 0015523343 scopus 로고
    • The reconstruction of a three-dimensional structure from projections and its application to electron microscopy II. Direct methods
    • Gilbert P.F. The reconstruction of a three-dimensional structure from projections and its application to electron microscopy II. Direct methods. Proc. R. Soc. London B Biol. Sci. 1972, 182:89-102.
    • (1972) Proc. R. Soc. London B Biol. Sci. , vol.182 , pp. 89-102
    • Gilbert, P.F.1
  • 27
    • 0001200282 scopus 로고
    • A new embedding medium for electron microscopy
    • Glauert A.M., Glauert R.H., Rogers G.E. A new embedding medium for electron microscopy. Nature 1956, 178:803.
    • (1956) Nature , vol.178 , pp. 803
    • Glauert, A.M.1    Glauert, R.H.2    Rogers, G.E.3
  • 29
    • 0030199056 scopus 로고    scopus 로고
    • Determination of the inelastic mean free path in ice by examination of tilted vesicles and automated most probable loss imaging
    • Grimm R., Typke D., Barmann M., Baumeister W. Determination of the inelastic mean free path in ice by examination of tilted vesicles and automated most probable loss imaging. Ultramicroscopy 1996, 63:169-179.
    • (1996) Ultramicroscopy , vol.63 , pp. 169-179
    • Grimm, R.1    Typke, D.2    Barmann, M.3    Baumeister, W.4
  • 31
    • 85019291339 scopus 로고
    • Electron densitometry of stained virus particles
    • Hall C.E. Electron densitometry of stained virus particles. J. Biophys. Biochem. Cytol. 1955, 1:1-12.
    • (1955) J. Biophys. Biochem. Cytol. , vol.1 , pp. 1-12
    • Hall, C.E.1
  • 32
    • 78649908289 scopus 로고    scopus 로고
    • Zernike phase contrast cryo-electron tomography of sodium-driven flagellar hook-basal bodies from Vibrio alginolyticus
    • Hosogi N., Shigematsu H., Terashima H., Homma M., Nagayama K. Zernike phase contrast cryo-electron tomography of sodium-driven flagellar hook-basal bodies from Vibrio alginolyticus. J. Struct. Biol. 2011, 173:67-76.
    • (2011) J. Struct. Biol. , vol.173 , pp. 67-76
    • Hosogi, N.1    Shigematsu, H.2    Terashima, H.3    Homma, M.4    Nagayama, K.5
  • 33
    • 38949130786 scopus 로고    scopus 로고
    • Electron cryo-tomographic structure of cystovirus phi 12
    • Hu G.B., Wei H., Rice W.J., Stokes D.L., Gottlieb P. Electron cryo-tomographic structure of cystovirus phi 12. Virology 2008, 372:1-9.
    • (2008) Virology , vol.372 , pp. 1-9
    • Hu, G.B.1    Wei, H.2    Rice, W.J.3    Stokes, D.L.4    Gottlieb, P.5
  • 34
    • 0742317562 scopus 로고
    • Some observations on the structure of tobacco mosaic virus
    • Almquist & Wiksell, Stockholm
    • Huxley H.E. Some observations on the structure of tobacco mosaic virus. Proceedings of the Stockholm Conference on Electron Microscopy 1956, 260-261. Almquist & Wiksell, Stockholm.
    • (1956) Proceedings of the Stockholm Conference on Electron Microscopy , pp. 260-261
    • Huxley, H.E.1
  • 36
    • 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
  • 37
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer J.R., Mastronarde D.N., McIntosh J.R. 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.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 38
    • 78651270028 scopus 로고    scopus 로고
    • Correlated fluorescence and 3D electron microscopy with high sensitivity and spatial precision
    • Kukulski W., Schorb M., Welsch S., Picco A., Kaksonen M., Briggs J.A. Correlated fluorescence and 3D electron microscopy with high sensitivity and spatial precision. J. Cell Biol. 2011, 192:111-119.
    • (2011) J. Cell Biol. , vol.192 , pp. 111-119
    • Kukulski, W.1    Schorb, M.2    Welsch, S.3    Picco, A.4    Kaksonen, M.5    Briggs, J.A.6
  • 42
    • 0015758617 scopus 로고
    • Caulobacter crescentus bacteriophage phiCbK: structure and in vitro self-assembly of the tail
    • Leonard K.R., Kleinschmidt A.K., Lake J.A. Caulobacter crescentus bacteriophage phiCbK: structure and in vitro self-assembly of the tail. J. Mol. Biol. 1973, 81:349-365.
    • (1973) J. Mol. Biol. , vol.81 , pp. 349-365
    • Leonard, K.R.1    Kleinschmidt, A.K.2    Lake, J.A.3
  • 43
    • 0020691376 scopus 로고
    • Electron microscopy of frozen biological suspensions
    • Lepault J., Booy F.P., Dubochet J. Electron microscopy of frozen biological suspensions. J. Microsc. 1983, 129:89-102.
    • (1983) J. Microsc. , vol.129 , pp. 89-102
    • Lepault, J.1    Booy, F.P.2    Dubochet, J.3
  • 45
    • 80051941010 scopus 로고    scopus 로고
    • Visualization of bacteriophage P1 infection by cryo-electron tomography of tiny Escherichia coli
    • Liu J., Chen C.-Y., Shiomi D., Niki H., Margolin W. Visualization of bacteriophage P1 infection by cryo-electron tomography of tiny Escherichia coli. Virology 2011, 417:304-311.
    • (2011) Virology , vol.417 , pp. 304-311
    • Liu, J.1    Chen, C.-Y.2    Shiomi, D.3    Niki, H.4    Margolin, W.5
  • 47
    • 14844330221 scopus 로고    scopus 로고
    • Structural studies by electron tomography: from cells to molecules
    • Lucic V., Forster 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
    • Lucic, V.1    Forster, F.2    Baumeister, W.3
  • 48
    • 48749089692 scopus 로고    scopus 로고
    • Cryo-electron tomography of cells: connecting structure and function
    • Lucic V., Leis A., Baumeister W. Cryo-electron tomography of cells: connecting structure and function. Histochem. Cell Biol. 2008, 130:185-196.
    • (2008) Histochem. Cell Biol. , vol.130 , pp. 185-196
    • Lucic, V.1    Leis, A.2    Baumeister, W.3
  • 49
    • 41549105310 scopus 로고
    • Improvements in epoxy resin embedding methods
    • Luft J.H. Improvements in epoxy resin embedding methods. J. Biophys. Biochem. Cytol. 1961, 9:409-414.
    • (1961) J. Biophys. Biochem. Cytol. , vol.9 , pp. 409-414
    • Luft, J.H.1
  • 50
    • 0031414675 scopus 로고    scopus 로고
    • Three-dimensional reconstruction from reduced sets of very noisy images acquired following a single-axis tilt schema: application of a new three-dimensional reconstruction algorithm and objective comparison with weighted backprojection
    • Marabini R., Rietzel E., Schroeder R., Herman G.T., Carazo J.M. Three-dimensional reconstruction from reduced sets of very noisy images acquired following a single-axis tilt schema: application of a new three-dimensional reconstruction algorithm and objective comparison with weighted backprojection. J. Struct. Biol. 1997, 120:363-371.
    • (1997) J. Struct. Biol. , vol.120 , pp. 363-371
    • Marabini, R.1    Rietzel, E.2    Schroeder, R.3    Herman, G.T.4    Carazo, J.M.5
  • 51
    • 33847685630 scopus 로고    scopus 로고
    • Focused-ion-beam thinning of frozen-hydrated biological specimens for cryo-electron microscopy
    • Marko M., Hsieh C., Schalek R., Frank J., Mannella C. Focused-ion-beam thinning of frozen-hydrated biological specimens for cryo-electron microscopy. Nat. Methods 2007, 4:215-217.
    • (2007) Nat. Methods , vol.4 , pp. 215-217
    • Marko, M.1    Hsieh, C.2    Schalek, R.3    Frank, J.4    Mannella, C.5
  • 52
    • 0034797254 scopus 로고    scopus 로고
    • Combined EM/X-ray imaging yields a quasi-atomic model of the adenovirus-related bacteriophage PRD1 and shows key capsid and membrane interactions
    • Martin C.S., Burnett R.M., de Haas F., Heinkel R., Rutten T., Fuller S.D., Butcher S.J., Bamford D.H. Combined EM/X-ray imaging yields a quasi-atomic model of the adenovirus-related bacteriophage PRD1 and shows key capsid and membrane interactions. Structure 2001, 9:917-930.
    • (2001) Structure , vol.9 , pp. 917-930
    • Martin, C.S.1    Burnett, R.M.2    de Haas, F.3    Heinkel, R.4    Rutten, T.5    Fuller, S.D.6    Butcher, S.J.7    Bamford, D.H.8
  • 53
    • 0031422417 scopus 로고    scopus 로고
    • Dual-axis tomography: an approach with alignment methods that preserve resolution
    • Mastronarde D.N. Dual-axis tomography: an approach with alignment methods that preserve resolution. J. Struct. Biol. 1997, 120:343-352.
    • (1997) J. Struct. Biol. , vol.120 , pp. 343-352
    • Mastronarde, D.N.1
  • 54
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde D.N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 2005, 152:36-51.
    • (2005) J. Struct. Biol. , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 55
    • 0020960227 scopus 로고
    • Electron microscopy of frozen hydrated sections of vitreous ice and vitrified biological samples
    • McDowall A.W., Chang J.J., Freeman R., Lepault J., Walter C.A., Dubochet J. Electron microscopy of frozen hydrated sections of vitreous ice and vitrified biological samples. J. Microsc. 1983, 131:1-9.
    • (1983) J. Microsc. , vol.131 , pp. 1-9
    • McDowall, A.W.1    Chang, J.J.2    Freeman, R.3    Lepault, J.4    Walter, C.A.5    Dubochet, J.6
  • 57
    • 33847176875 scopus 로고    scopus 로고
    • Correlative light and electron microscopy of early Caenorhabditis elegans embryos in mitosis
    • Muller-Reichert T., Srayko M., Hyman A., O'Toole E.T., McDonald K. Correlative light and electron microscopy of early Caenorhabditis elegans embryos in mitosis. Methods Cell Biol. 2007, 79:101-119.
    • (2007) Methods Cell Biol. , vol.79 , pp. 101-119
    • Muller-Reichert, T.1    Srayko, M.2    Hyman, A.3    O'Toole, E.T.4    McDonald, K.5
  • 58
    • 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
  • 59
    • 35648949977 scopus 로고    scopus 로고
    • Electron cryotomography
    • 415, 417 passim
    • Murphy G.E., Jensen G.J. Electron cryotomography. Biotechniques 2007, 43(4):413. 415, 417 passim.
    • (2007) Biotechniques , vol.43 , Issue.4 , pp. 413
    • Murphy, G.E.1    Jensen, G.J.2
  • 60
    • 81355160170 scopus 로고    scopus 로고
    • Stepwise expansion of the bacteriophage φ6 procapsid: possible packaging intermediates
    • Nemecek D., Cheng N., Qiao J., Mindich L., Steven A.C., Heymann J.B. Stepwise expansion of the bacteriophage φ6 procapsid: possible packaging intermediates. J. Mol. Biol. 2011, 414:260-271.
    • (2011) J. Mol. Biol. , vol.414 , pp. 260-271
    • Nemecek, D.1    Cheng, N.2    Qiao, J.3    Mindich, L.4    Steven, A.C.5    Heymann, J.B.6
  • 61
    • 77955085566 scopus 로고    scopus 로고
    • Cryo-electron tomography of bacteriophage [phi]6 procapsids shows random occupancy of the binding sites for RNA polymerase and packaging NTPase
    • Nemecek D., Heymann J.B., Qiao J., Mindich L., Steven A.C. Cryo-electron tomography of bacteriophage [phi]6 procapsids shows random occupancy of the binding sites for RNA polymerase and packaging NTPase. J. Struct. Biol. 2010, 171:389-396.
    • (2010) J. Struct. Biol. , vol.171 , pp. 389-396
    • Nemecek, D.1    Heymann, J.B.2    Qiao, J.3    Mindich, L.4    Steven, A.C.5
  • 63
    • 65449162388 scopus 로고    scopus 로고
    • Correlative cryo-light microscopy and cryo-electron tomography: from cellular territories to molecular landscapes
    • Plitzko J.M., Rigort A., Leis A. Correlative cryo-light microscopy and cryo-electron tomography: from cellular territories to molecular landscapes. Curr. Opin. Biotechnol. 2009, 20:83-89.
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 83-89
    • Plitzko, J.M.1    Rigort, A.2    Leis, A.3
  • 64
    • 85025399883 scopus 로고
    • A study of tissue culture cells by electron microscopy: methods and preliminary observations
    • Porter K.R., Claude A., Fullam E.F. A study of tissue culture cells by electron microscopy: methods and preliminary observations. J. Exp. Med. 1945, 81:233-246.
    • (1945) J. Exp. Med. , vol.81 , pp. 233-246
    • Porter, K.R.1    Claude, A.2    Fullam, E.F.3
  • 65
    • 0014258007 scopus 로고
    • Primary adsorption site of phage PBS1: the flagellum of Bacillus subtilis
    • Raimondo L.M., Lundh N.P., Martinez R.J. Primary adsorption site of phage PBS1: the flagellum of Bacillus subtilis. J. Virol. 1968, 2:256-264.
    • (1968) J. Virol. , vol.2 , pp. 256-264
    • Raimondo, L.M.1    Lundh, N.P.2    Martinez, R.J.3
  • 66
    • 0042887681 scopus 로고    scopus 로고
    • Comparative analysis of bacterial viruses Bam35, infecting a gram-positive host, and PRD1, infecting gram-negative hosts, demonstrates a viral lineage
    • Ravantti J.J., Gaidelyte A., Bamford D.H., Bamford J.K.H. Comparative analysis of bacterial viruses Bam35, infecting a gram-positive host, and PRD1, infecting gram-negative hosts, demonstrates a viral lineage. Virology 2003, 313:401-414.
    • (2003) Virology , vol.313 , pp. 401-414
    • Ravantti, J.J.1    Gaidelyte, A.2    Bamford, D.H.3    Bamford, J.K.H.4
  • 67
    • 35148839574 scopus 로고    scopus 로고
    • Correlative microscopy: bridging the gap between fluorescence light microscopy and cryo-electron tomography
    • Sartori A., Gatz R., Beck F., Rigort A., Baumeister W., Plitzko J.M. Correlative microscopy: bridging the gap between fluorescence light microscopy and cryo-electron tomography. J. Struct. Biol. 2007, 160:135-145.
    • (2007) J. Struct. Biol. , vol.160 , pp. 135-145
    • Sartori, A.1    Gatz, R.2    Beck, F.3    Rigort, A.4    Baumeister, W.5    Plitzko, J.M.6
  • 68
    • 0014099357 scopus 로고
    • How bacteriophage chi attacks motile bacteria
    • Schade S.Z., Adler J., Ris H. How bacteriophage chi attacks motile bacteria. J. Virol. 1967, 1:599-609.
    • (1967) J. Virol. , vol.1 , pp. 599-609
    • Schade, S.Z.1    Adler, J.2    Ris, H.3
  • 69
    • 40649109028 scopus 로고    scopus 로고
    • Methods for aligning and for averaging 3D volumes with missing data
    • Schmid M.F., Booth C.R. 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.F.1    Booth, C.R.2
  • 72
    • 0016391518 scopus 로고
    • Electron diffraction of frozen, hydrated protein crystals
    • Taylor K.A., Glaeser R.M. Electron diffraction of frozen, hydrated protein crystals. Science 1974, 186:1036-1037.
    • (1974) Science , vol.186 , pp. 1036-1037
    • Taylor, K.A.1    Glaeser, R.M.2
  • 73
    • 69949083343 scopus 로고    scopus 로고
    • Tools for correlative cryo-fluorescence microscopy and cryo-electron tomography applied to whole mitochondria in human endothelial cells
    • van Driel L.F., Valentijn J.A., Valentijn K.M., Koning R.I., Koster A.J. Tools for correlative cryo-fluorescence microscopy and cryo-electron tomography applied to whole mitochondria in human endothelial cells. Eur. J. Cell. Biol. 2009, 88:669-684.
    • (2009) Eur. J. Cell. Biol. , vol.88 , pp. 669-684
    • van Driel, L.F.1    Valentijn, J.A.2    Valentijn, K.M.3    Koning, R.I.4    Koster, A.J.5
  • 74
    • 85011200555 scopus 로고
    • Staining of tissue sections for electron microscopy with heavy metals
    • Watson M.L. Staining of tissue sections for electron microscopy with heavy metals. J. Biophys. Biochem. Cytol. 1958, 4:475-478.
    • (1958) J. Biophys. Biochem. Cytol. , vol.4 , pp. 475-478
    • Watson, M.L.1
  • 75
    • 0000523688 scopus 로고
    • Staining of tissue sections for electron microscopy with heavy metals. II. Application of solutions containing lead and barium
    • Watson M.L. Staining of tissue sections for electron microscopy with heavy metals. II. Application of solutions containing lead and barium. J. Biophys. Biochem. Cytol. 1958, 4:727-730.
    • (1958) J. Biophys. Biochem. Cytol. , vol.4 , pp. 727-730
    • Watson, M.L.1
  • 76
    • 34247185183 scopus 로고    scopus 로고
    • Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells
    • Wright E.R., Schooler J.B., Ding H.J., Kieffer C., Fillmore C., Sundquist W.I., Jensen G.J. Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells. EMBO J. 2007, 26:2218-2226.
    • (2007) EMBO J. , vol.26 , pp. 2218-2226
    • Wright, E.R.1    Schooler, J.B.2    Ding, H.J.3    Kieffer, C.4    Fillmore, C.5    Sundquist, W.I.6    Jensen, G.J.7
  • 77
    • 80053563027 scopus 로고    scopus 로고
    • Cryo-electron tomography: gaining insight into cellular processes by structural approaches
    • Yahav T., Maimon T., Grossman E., Dahan I., Medalia O. Cryo-electron tomography: gaining insight into cellular processes by structural approaches. Curr. Opin. Struct. Biol. 2011, 21:670-677.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 670-677
    • Yahav, T.1    Maimon, T.2    Grossman, E.3    Dahan, I.4    Medalia, O.5
  • 78
    • 33748038359 scopus 로고    scopus 로고
    • Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ
    • Zanetti G., Briggs J.A., Grunewald K., Sattentau Q.J., Fuller S.D. Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ. PLoS Pathog. 2006, 2:e83.
    • (2006) PLoS Pathog. , vol.2
    • Zanetti, G.1    Briggs, J.A.2    Grunewald, K.3    Sattentau, Q.J.4    Fuller, S.D.5
  • 79
    • 2942608087 scopus 로고    scopus 로고
    • An improved strategy for automated electron microscopic tomography
    • Zheng Q.S., Braunfeld M.B., Sedat J.W., Agard D.A. An improved strategy for automated electron microscopic tomography. J. Struct Biol. 2004, 147:91-101.
    • (2004) J. Struct Biol. , vol.147 , pp. 91-101
    • Zheng, Q.S.1    Braunfeld, M.B.2    Sedat, J.W.3    Agard, D.A.4
  • 80
    • 57149107577 scopus 로고    scopus 로고
    • Cryoelectron tomography of HIV-1 envelope spikes: further evidence for tripod-like legs
    • Zhu P., Winkler H., Chertova E., Taylor K.A., Roux K.H. Cryoelectron tomography of HIV-1 envelope spikes: further evidence for tripod-like legs. PLoS Pathog. 2008, 4:e1000203.
    • (2008) PLoS Pathog. , vol.4
    • Zhu, P.1    Winkler, H.2    Chertova, E.3    Taylor, K.A.4    Roux, K.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.