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Volumn 68, Issue , 2013, Pages 203-246

Combined approaches to study virus structures

Author keywords

Bacteriophage; Capsid; Cryo electron microscopy; Cryo electron tomography; Crystal structure; Dissociation; Electron microscopy; Electron tomography; Fitting; Hybrid methods; Mutagenesis; Small angle X ray scattering; Virus; X ray crystallography

Indexed keywords

ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; ELECTRON MICROSCOPY; HUMAN; REVIEW; ULTRASTRUCTURE; VIRUS; X RAY CRYSTALLOGRAPHY;

EID: 84887354081     PISSN: 03060225     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-94-007-6552-8_7     Document Type: Article
Times cited : (2)

References (129)
  • 3
    • 0023059423 scopus 로고
    • Three-dimensional structure of the adenovirus major coat protein hexon
    • Roberts MM, White JL, Grutter MG, Burnett RM (1986) Three-dimensional structure of the adenovirus major coat protein hexon. Science 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
  • 4
    • 70449130792 scopus 로고    scopus 로고
    • Modern uses of electron microscopy for detection of viruses
    • Goldsmith CS, Miller SE (2009) Modern uses of electron microscopy for detection of viruses. Clin Microbiol Rev 22:552-563
    • (2009) Clin Microbiol Rev , vol.22 , pp. 552-563
    • Goldsmith, C.S.1    Miller, S.E.2
  • 5
    • 39849102970 scopus 로고    scopus 로고
    • Backbone structure of the infectious epsilon15 virus capsid revealed by electron cryomicroscopy
    • Jiang W, Baker ML, Jakana J, Weigele PR, King J, ChiuW (2008) Backbone structure of the infectious epsilon15 virus capsid revealed by electron cryomicroscopy. Nature 451:1130-1134
    • (2008) Nature , vol.451 , pp. 1130-1134
    • Jiang, W.1    Baker, M.L.2    Jakana, J.3    Weigele, P.R.4    King, J.5    Chiu, W.6
  • 7
    • 0242571958 scopus 로고    scopus 로고
    • Small-angle scattering studies of biological macromolecules in solution
    • Svergun DI, Koch MH (2003) Small-angle scattering studies of biological macromolecules in solution. Rep Prog Phys 66:1735-1782
    • (2003) Rep Prog Phys , vol.66 , pp. 1735-1782
    • Svergun, D.I.1    Koch, M.H.2
  • 8
    • 0036816606 scopus 로고    scopus 로고
    • Advances in structure analysis using small-angle scattering in solution
    • Svergun DI, Koch MH (2002) Advances in structure analysis using small-angle scattering in solution. Curr Opin Struct Biol 12:654-660
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 654-660
    • Svergun, D.I.1    Koch, M.H.2
  • 9
    • 0035192552 scopus 로고    scopus 로고
    • Fibre diffraction studies of filamentous viruses
    • Stubbs G (2001) Fibre diffraction studies of filamentous viruses. Rep Prog Phys 64:1389-1425
    • (2001) Rep Prog Phys , vol.64 , pp. 1389-1425
    • Stubbs, G.1
  • 12
    • 0035943387 scopus 로고    scopus 로고
    • Analysis of rapid, large-scale protein quaternary structural changes: Time-resolved X-ray solution scattering of Nudaurelia capensis omega virus (NomegaV) maturation
    • Canady MA, Tsuruta H, Johnson JE (2001) Analysis of rapid, large-scale protein quaternary structural changes: time-resolved X-ray solution scattering of Nudaurelia capensis omega virus (NomegaV) maturation. J Mol Biol 311:803-814
    • (2001) J Mol Biol , vol.311 , pp. 803-814
    • Canady, M.A.1    Tsuruta, H.2    Johnson, J.E.3
  • 15
    • 0022409872 scopus 로고
    • Three-dimensional structure of poliovirus at 2.9 A resolution
    • Hogle JM, Chow M, Filman DJ (1985) Three-dimensional structure of poliovirus at 2.9 A resolution. Science 229:1358-1365
    • (1985) Science , vol.229 , pp. 1358-1365
    • Hogle, J.M.1    Chow, M.2    Filman, D.J.3
  • 19
    • 77956098333 scopus 로고    scopus 로고
    • Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks
    • Liu H, Jin L, Koh SB, Atanasov I, Schein S, Wu L, Zhou ZH (2010) Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks. Science 329:1038-1043
    • (2010) Science , vol.329 , pp. 1038-1043
    • Liu, H.1    Jin, L.2    Koh, S.B.3    Atanasov, I.4    Schein, S.5    Wu, L.6    Zhou, Z.H.7
  • 20
    • 77956128250 scopus 로고    scopus 로고
    • Crystal structure of human adenovirus at 3.5 A resolution
    • Reddy VS, Natchiar SK, Stewart PL, Nemerow GR (2010) Crystal structure of human adenovirus at 3.5 A resolution. Science 329:1071-1075
    • (2010) Science , vol.329 , pp. 1071-1075
    • Reddy, V.S.1    Natchiar, S.K.2    Stewart, P.L.3    Nemerow, G.R.4
  • 24
    • 79953733320 scopus 로고    scopus 로고
    • The design of macromolecular crystallography diffraction experiments
    • Evans G, Axford D, Owen RL (2011) The design of macromolecular crystallography diffraction experiments. Acta Crystallogr D Biol Crystallogr 67:261-270
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 261-270
    • Evans, G.1    Axford, D.2    Owen, R.L.3
  • 25
    • 0033780164 scopus 로고    scopus 로고
    • Fitting atomic models into electron-microscopy maps
    • Rossmann MG (2000) Fitting atomic models into electron-microscopy maps. Acta Crystallogr D Biol Crystallogr 56:1341-1349
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , pp. 1341-1349
    • Rossmann, M.G.1
  • 26
    • 0033571522 scopus 로고    scopus 로고
    • Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor
    • Kolatkar PR, Bella J, Olson NH, Bator CM, Baker TS, Rossmann MG (1999) Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor. EMBO J 18:6249-6259
    • (1999) EMBO J , vol.18 , pp. 6249-6259
    • Kolatkar, P.R.1    Bella, J.2    Olson, N.H.3    Bator, C.M.4    Baker, T.S.5    Rossmann, M.G.6
  • 27
    • 0042827240 scopus 로고    scopus 로고
    • Hybrid vigor: Hybrid methods in viral structure determination
    • Gilbert RJ, Grimes JM, Stuart DI (2003) Hybrid vigor: hybrid methods in viral structure determination. Adv Protein Chem 64:37-91
    • (2003) Adv Protein Chem , vol.64 , pp. 37-91
    • Gilbert, R.J.1    Grimes, J.M.2    Stuart, D.I.3
  • 28
    • 25844459522 scopus 로고    scopus 로고
    • Combining electron microscopy and comparative protein structure modeling
    • Topf M, Sali A (2005) Combining electron microscopy and comparative protein structure modeling. Curr Opin Struct Biol 15:578-585
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 578-585
    • Topf, M.1    Sali, A.2
  • 31
    • 8244249460 scopus 로고    scopus 로고
    • Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: Positioning of a highly mobile antigenic loop
    • Hewat EA, Verdaguer N, Fita I, Blakemore W, Brookes S, King A, Newman J, Domingo E, Mateu MG, Stuart DI (1997) Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: positioning of a highly mobile antigenic loop. EMBO J 16:1492-1500
    • (1997) EMBO J , vol.16 , pp. 1492-1500
    • Hewat, E.A.1    Verdaguer, N.2    Fita, I.3    Blakemore, W.4    Brookes, S.5    King, A.6    Newman, J.7    Domingo, E.8    Mateu, M.G.9    Stuart, D.I.10
  • 33
    • 41349112506 scopus 로고    scopus 로고
    • The flavivirus precursor membrane-envelope protein complex: Structure and maturation
    • Li L, Lok SM, Yu IM, Zhang Y, Kuhn RJ, Chen J, Rossmann MG (2008) The flavivirus precursor membrane-envelope protein complex: structure and maturation. Science 319:1830-1834
    • (2008) Science , vol.319 , pp. 1830-1834
    • Li, L.1    Lok, S.M.2    Yu, I.M.3    Zhang, Y.4    Kuhn, R.J.5    Chen, J.6    Rossmann, M.G.7
  • 35
    • 0029159163 scopus 로고
    • Bacteriophage PRD1: A broad host range dsDNA tectivirus with an internal membrane
    • Bamford DH, Caldentey J, Bamford JK (1995) Bacteriophage PRD1: a broad host range dsDNA tectivirus with an internal membrane. Adv Virus Res 45:281-319
    • (1995) Adv Virus Res , vol.45 , pp. 281-319
    • Bamford, D.H.1    Caldentey, J.2    Bamford, J.K.3
  • 36
    • 0034797254 scopus 로고    scopus 로고
    • Combined EM/X-Ray imaging yields a quasi-atomic model of the adenovirusrelated bacteriophage PRD1 and shows key capsid and membrane interactions
    • San Martin C, Burnett RM, de Haas F, Heinkel R, Rutten T, Fuller SD, Butcher SJ, Bamford DH (2001) Combined EM/X-Ray imaging yields a quasi-atomic model of the adenovirusrelated bacteriophage PRD1 and shows key capsid and membrane interactions. Structure 9:917-930
    • (2001) Structure , vol.9 , pp. 917-930
    • San Martin, C.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
  • 37
    • 0033578669 scopus 로고    scopus 로고
    • Viral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures
    • Benson SD, Bamford JK, Bamford DH, Burnett RM (1999) Viral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures. Cell 98:825-833
    • (1999) Cell , vol.98 , pp. 825-833
    • Benson, S.D.1    Bamford, J.K.2    Bamford, D.H.3    Burnett, R.M.4
  • 40
    • 71049139404 scopus 로고    scopus 로고
    • Averaging of electron subtomograms and random conical tilt reconstructions through likelihood optimization
    • Scheres SH, Melero R, Valle M, Carazo JM (2009) Averaging of electron subtomograms and random conical tilt reconstructions through likelihood optimization. Structure 17:1563-1572
    • (2009) Structure , vol.17 , pp. 1563-1572
    • Scheres, S.H.1    Melero, R.2    Valle, M.3    Carazo, J.M.4
  • 41
    • 84860574289 scopus 로고    scopus 로고
    • Dynamo: A flexible, userfriendly development tool for subtomogram averaging of cryo-EM data in high-performance computing environments
    • Castanõ-Diez D, Kudryashev M, Arheit M, Stahlberg H (2012) Dynamo: a flexible, userfriendly development tool for subtomogram averaging of cryo-EM data in high-performance computing environments. J Struct Biol 178:139-151
    • (2012) J Struct Biol , vol.178 , pp. 139-151
    • Castanõ-Diez, D.1    Kudryashev, M.2    Arheit, M.3    Stahlberg, H.4
  • 44
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger AT (1992) Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355:472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 45
    • 0001121107 scopus 로고
    • Ab initio phase determination for viruses with high symmetry: A feasibility study
    • Tsao J, Chapman MS, Rossmann MG (1992) Ab initio phase determination for viruses with high symmetry: a feasibility study. Acta Crystallogr A 48(Pt 3):293-301
    • (1992) Acta Crystallogr A , vol.48 , pp. 293-301
    • Tsao, J.1    Chapman, M.S.2    Rossmann, M.G.3
  • 46
    • 0001121111 scopus 로고
    • Ab initio phase determination for spherical viruses: Parameter determination for spherical-shell models
    • Chapman MS, Tsao J, Rossmann MG (1992) Ab initio phase determination for spherical viruses: parameter determination for spherical-shell models. Acta Crystallogr A 48(Pt 3): 301-312
    • (1992) Acta Crystallogr A , vol.48 , pp. 301-312
    • Chapman, M.S.1    Tsao, J.2    Rossmann, M.G.3
  • 47
    • 0028865296 scopus 로고
    • Ab initio phase determination and phase extension using noncrystallographic symmetry
    • Rossmann MG (1995) Ab initio phase determination and phase extension using noncrystallographic symmetry. Curr Opin Struct Biol 5:650-655
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 650-655
    • Rossmann, M.G.1
  • 48
    • 84944817135 scopus 로고
    • The molecular replacement method
    • Rossmann MG (1990) The molecular replacement method. Acta Crystallogr A 46(Pt 2):73-82
    • (1990) Acta Crystallogr A , vol.46 , pp. 73-82
    • Rossmann, M.G.1
  • 49
    • 0024578406 scopus 로고
    • The three-dimensional structure of foot-and-mouth disease virus at 2.9 Åresolution
    • Acharya R, Fry E, Stuart D, Fox G, Rowlands D, Brown F (1989) The three-dimensional structure of foot-and-mouth disease virus at 2.9 Åresolution. Nature 337:709-716
    • (1989) Nature , vol.337 , pp. 709-716
    • Acharya, R.1    Fry, E.2    Stuart, D.3    Fox, G.4    Rowlands, D.5    Brown, F.6
  • 50
    • 0028881913 scopus 로고
    • Crystal structure of Pseudomonas aeruginosa catabolic ornithine transcarbamoylase at 3.0 Åresolution: A different oligomeric organization in the transcarbamoylase family
    • Villeret V, Tricot C, Stalon V, Dideberg O (1995) Crystal structure of Pseudomonas aeruginosa catabolic ornithine transcarbamoylase at 3.0 Åresolution: a different oligomeric organization in the transcarbamoylase family. Proc Natl Acad Sci U S A 92:10762-10766
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 10762-10766
    • Villeret, V.1    Tricot, C.2    Stalon, V.3    Dideberg, O.4
  • 51
    • 0035788356 scopus 로고    scopus 로고
    • Using electron-microscopy images as a model for molecular replacement
    • Dodson EJ (2001) Using electron-microscopy images as a model for molecular replacement. Acta Crystallogr D Biol Crystallogr 57:1405-1409
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 1405-1409
    • Dodson, E.J.1
  • 52
    • 37349034299 scopus 로고    scopus 로고
    • Combining X-ray and electron-microscopy data to solve crystal structures
    • Navaza J (2008) Combining X-ray and electron-microscopy data to solve crystal structures. Acta Crystallogr D Biol Crystallogr 64:70-75
    • (2008) Acta Crystallogr D Biol Crystallogr , vol.64 , pp. 70-75
    • Navaza, J.1
  • 53
    • 77952032301 scopus 로고    scopus 로고
    • Macromolecular crystal data phased by negative-stained electron-microscopy reconstructions
    • Trapani S, Schoehn G, Navaza J, Abergel C (2010) Macromolecular crystal data phased by negative-stained electron-microscopy reconstructions. Acta Crystallogr D Biol Crystallogr 66:514-521
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 514-521
    • Trapani, S.1    Schoehn, G.2    Navaza, J.3    Abergel, C.4
  • 55
    • 4344559453 scopus 로고    scopus 로고
    • The PM2 virion has a novel organization with an internal membrane and pentameric receptor binding spikes
    • Huiskonen JT, Kivelä HM, Bamford DH, Butcher SJ (2004) The PM2 virion has a novel organization with an internal membrane and pentameric receptor binding spikes. Nat Struct Mol Biol 11:850-856
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 850-856
    • Huiskonen, J.T.1    Kivelä, H.M.2    Bamford, D.H.3    Butcher, S.J.4
  • 56
    • 79952267049 scopus 로고    scopus 로고
    • The use of low-resolution phasing followed by phase extension from 7.6 to 2.5 Åresolution with noncrystallographic symmetry to solve the structure of a bacteriophage capsid protein
    • Abrescia NG, Grimes JM, Oksanen HM, Bamford JK, Bamford DH, Stuart DI (2011) The use of low-resolution phasing followed by phase extension from 7.6 to 2.5 Åresolution with noncrystallographic symmetry to solve the structure of a bacteriophage capsid protein. Acta Crystallogr D Biol Crystallogr 67:228-232
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 228-232
    • Abrescia, N.G.1    Grimes, J.M.2    Oksanen, H.M.3    Bamford, J.K.4    Bamford, D.H.5    Stuart, D.I.6
  • 58
    • 84857966803 scopus 로고    scopus 로고
    • Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography
    • Leitner A, Reischl R, Walzthoeni T, Herzog F, Bohn S, Förster F, Aebersold R (2012) Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography. Mol Cell Proteomics 11(M111):014126
    • (2012) Mol Cell Proteomics , vol.11 , Issue.M111
    • Leitner, A.1    Reischl, R.2    Walzthoeni, T.3    Herzog, F.4    Bohn, S.5    Förster, F.6    Aebersold, R.7
  • 59
    • 0038758998 scopus 로고    scopus 로고
    • The tailless icosahedral membrane virus PRD1 localizes the proteins involved in genome packaging and injection at a unique vertex
    • Gowen B, Bamford JK, Bamford DH, Fuller SD (2003) The tailless icosahedral membrane virus PRD1 localizes the proteins involved in genome packaging and injection at a unique vertex. J Virol 77:7863-7871
    • (2003) J Virol , vol.77 , pp. 7863-7871
    • Gowen, B.1    Bamford, J.K.2    Bamford, D.H.3    Fuller, S.D.4
  • 60
    • 0038523777 scopus 로고    scopus 로고
    • The unique vertex of bacterial virus PRD1 is connected to the viral internal membrane
    • Strömsten NJ, Bamford DH, Bamford JK (2003) The unique vertex of bacterial virus PRD1 is connected to the viral internal membrane. J Virol 77:6314-6321
    • (2003) J Virol , vol.77 , pp. 6314-6321
    • Strömsten, N.J.1    Bamford, D.H.2    Bamford, J.K.3
  • 61
    • 38949096838 scopus 로고    scopus 로고
    • Genetics for Pseudoalteromonas provides tools to manipulate marine bacterial virus PM2
    • Kivelä HM, Madonna S, Krupovic M, Tutino ML, Bamford JK (2008) Genetics for Pseudoalteromonas provides tools to manipulate marine bacterial virus PM2. J Bacteriol 190:1298-1307
    • (2008) J Bacteriol , vol.190 , pp. 1298-1307
    • Kivelä, H.M.1    Madonna, S.2    Krupovic, M.3    Tutino, M.L.4    Bamford, J.K.5
  • 62
    • 84857097120 scopus 로고    scopus 로고
    • Replicationcompetent influenza A virus that encodes a split-green fluorescent protein-tagged PB2 polymerase subunit allows live-cell imaging of the virus life cycle
    • Avilov SV, Moisy D, Munier S, Schraidt O, Naffakh N, Cusack S (2011) Replicationcompetent influenza A virus that encodes a split-green fluorescent protein-tagged PB2 polymerase subunit allows live-cell imaging of the virus life cycle. J Virol 86:1433-1448
    • (2011) J Virol , vol.86 , pp. 1433-1448
    • Avilov, S.V.1    Moisy, D.2    Munier, S.3    Schraidt, O.4    Naffakh, N.5    Cusack, S.6
  • 63
    • 38349051304 scopus 로고    scopus 로고
    • Selenomethionine labeling of large biological macromolecular complexes: Probing the structure of marine bacterial virus PM2
    • Kivelä HM, Abrescia NG, Bamford JK, Grimes JM, Stuart DI, Bamford DH (2008) Selenomethionine labeling of large biological macromolecular complexes: probing the structure of marine bacterial virus PM2. J Struct Biol 161:204-210
    • (2008) J Struct Biol , vol.161 , pp. 204-210
    • Kivelä, H.M.1    Abrescia, N.G.2    Bamford, J.K.3    Grimes, J.M.4    Stuart, D.I.5    Bamford, D.H.6
  • 64
    • 0020451646 scopus 로고
    • Structure of the lipid-containing bacteriophage PRD1: Disruption of wild-type and nonsense mutant phage particles with guanidine hydrochloride
    • Bamford D, Mindich L (1982) Structure of the lipid-containing bacteriophage PRD1: disruption of wild-type and nonsense mutant phage particles with guanidine hydrochloride. J Virol 44:1031-1038
    • (1982) J Virol , vol.44 , pp. 1031-1038
    • Bamford, D.1    Mindich, L.2
  • 65
    • 0036319176 scopus 로고    scopus 로고
    • Bacteriophage PM2 has a protein capsid surrounding a spherical proteinaceous lipid core
    • Kivelä HM, Kalkkinen N, Bamford DH (2002) Bacteriophage PM2 has a protein capsid surrounding a spherical proteinaceous lipid core. J Virol 76:8169-8178
    • (2002) J Virol , vol.76 , pp. 8169-8178
    • Kivelä, H.M.1    Kalkkinen, N.2    Bamford, D.H.3
  • 66
    • 0027198788 scopus 로고
    • Dissociation of the lipid-containing bacteriophage PRD1: Effects of heat, pH, and sodium dodecyl sulfate
    • Caldentey J, Luo C, Bamford DH (1993) Dissociation of the lipid-containing bacteriophage PRD1: effects of heat, pH, and sodium dodecyl sulfate. Virology 194:557-563
    • (1993) Virology , vol.194 , pp. 557-563
    • Caldentey, J.1    Luo, C.2    Bamford, D.H.3
  • 67
    • 33750991064 scopus 로고    scopus 로고
    • Quantitative dissociation of archaeal virus SH1 reveals distinct capsid proteins and a lipid core
    • Kivelä HM, Roine E, Kukkaro P, Laurinavicius S, Somerharju P, Bamford DH (2006) Quantitative dissociation of archaeal virus SH1 reveals distinct capsid proteins and a lipid core. Virology 356:4-11
    • (2006) Virology , vol.356 , pp. 4-11
    • Kivelä, H.M.1    Roine, E.2    Kukkaro, P.3    Laurinavicius, S.4    Somerharju, P.5    Bamford, D.H.6
  • 69
    • 84862583038 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of the major capsid proteins VP16 and VP17 of bacteriophage P23-77
    • Rissanen I, Pawlowski A, Harlos K, Grimes JM, Stuart DI, Bamford JKH (2012) Crystallization and preliminary crystallographic analysis of the major capsid proteins VP16 and VP17 of bacteriophage P23-77. Acta Crystallogr F68:580-583
    • (2012) Acta Crystallogr F , vol.68 , pp. 580-583
    • Rissanen, I.1    Pawlowski, A.2    Harlos, K.3    Grimes, J.M.4    Stuart, D.I.5    Bamford, J.K.H.6
  • 70
    • 33745912405 scopus 로고    scopus 로고
    • A time- and cost-efficient system for high-level protein production in mammalian cells
    • Aricescu AR, Lu W, Jones EY (2006) A time- and cost-efficient system for high-level protein production in mammalian cells. Acta Crystallogr D Biol Crystallogr 62:1243-1250
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 1243-1250
    • Aricescu, A.R.1    Lu, W.2    Jones, E.Y.3
  • 71
    • 0036006764 scopus 로고    scopus 로고
    • The X-ray crystal structure of P3, the major coat protein of the lipid-containing bacteriophage PRD1, at 1.65 A resolution
    • Benson SD, Bamford JK, Bamford DH, Burnett RM (2002) The X-ray crystal structure of P3, the major coat protein of the lipid-containing bacteriophage PRD1, at 1.65 A resolution. Acta Crystallogr D Biol Crystallogr 58:39-59
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 39-59
    • Benson, S.D.1    Bamford, J.K.2    Bamford, D.H.3    Burnett, R.M.4
  • 72
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson WA (1991) Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254:51-58
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 73
    • 73649136056 scopus 로고    scopus 로고
    • DNA heats up: Energetics of genome ejection from phage revealed by isothermal titration calorimetry
    • Jeembaeva M, Jonsson B, Castelnovo M, Evilevitch A (2010) DNA heats up: energetics of genome ejection from phage revealed by isothermal titration calorimetry. J Mol Biol 395:1079-1087
    • (2010) J Mol Biol , vol.395 , pp. 1079-1087
    • Jeembaeva, M.1    Jonsson, B.2    Castelnovo, M.3    Evilevitch, A.4
  • 76
    • 14844330221 scopus 로고    scopus 로고
    • Structural studies by electron tomography: From cells to molecules
    • Lucic V, Forster F, Baumeister W (2005) Structural studies by electron tomography: from cells to molecules. Annu Rev Biochem 74:833-865
    • (2005) Annu Rev Biochem , vol.74 , pp. 833-865
    • Lucic, V.1    Forster, F.2    Baumeister, W.3
  • 78
    • 55249110450 scopus 로고    scopus 로고
    • Threedimensional organization of Rift Valley fever virus revealed by cryoelectron tomography
    • Freiberg AN, Sherman MB, Morais MC, Holbrook MR, Watowich SJ (2008) Threedimensional organization of Rift Valley fever virus revealed by cryoelectron tomography. J Virol 82:10341-10348
    • (2008) J Virol , vol.82 , pp. 10341-10348
    • Freiberg, A.N.1    Sherman, M.B.2    Morais, M.C.3    Holbrook, M.R.4    Watowich, S.J.5
  • 81
    • 27744487093 scopus 로고    scopus 로고
    • Common ancestry of herpesviruses and tailed DNA bacteriophages
    • Baker ML, Jiang W, Rixon FJ, Chiu W (2005) Common ancestry of herpesviruses and tailed DNA bacteriophages. J Virol 79:14967-14970
    • (2005) J Virol , vol.79 , pp. 14967-14970
    • Baker, M.L.1    Jiang, W.2    Rixon, F.J.3    Chiu, W.4
  • 82
    • 35148838173 scopus 로고    scopus 로고
    • Single particle cryoelectron tomography characterization of the structure and structural variability of poliovirus- receptor-membrane complex at 30 A resolution
    • Bostina M, Bubeck D, Schwartz C, Nicastro D, Filman DJ, Hogle JM (2007) Single particle cryoelectron tomography characterization of the structure and structural variability of poliovirus- receptor-membrane complex at 30 A resolution. J Struct Biol 160:200-210
    • (2007) J Struct Biol , vol.160 , pp. 200-210
    • Bostina, M.1    Bubeck, D.2    Schwartz, C.3    Nicastro, D.4    Filman, D.J.5    Hogle, J.M.6
  • 88
    • 64049094507 scopus 로고    scopus 로고
    • Electron cryo-microscopy and single-particle averaging of Rift Valley fever virus: Evidence for GN-GC glycoprotein heterodimers
    • Huiskonen JT, Overby AK, Weber F, Grünewald K (2009) Electron cryo-microscopy and single-particle averaging of Rift Valley fever virus: evidence for GN-GC glycoprotein heterodimers. J Virol 83:3762-3769
    • (2009) J Virol , vol.83 , pp. 3762-3769
    • Huiskonen, J.T.1    Overby, A.K.2    Weber, F.3    Grünewald, K.4
  • 90
    • 75049083128 scopus 로고    scopus 로고
    • How baculovirus polyhedra fit square pegs into round holes to robustly package viruses
    • Ji X, Sutton G, Evans G, Axford D, Owen R, Stuart DI (2009) How baculovirus polyhedra fit square pegs into round holes to robustly package viruses. EMBO J 29:505-514
    • (2009) EMBO J , vol.29 , pp. 505-514
    • Ji, X.1    Sutton, G.2    Evans, G.3    Axford, D.4    Owen, R.5    Stuart, D.I.6
  • 92
    • 78049444131 scopus 로고    scopus 로고
    • Electron tomography of the supramolecular structure of virusinfected cells
    • Iwasaki K, Omura T (2010) Electron tomography of the supramolecular structure of virusinfected cells. Curr Opin Struct Biol 20:632-639
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 632-639
    • Iwasaki, K.1    Omura, T.2
  • 96
    • 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 GD, Zhang J, Goddard TD, Chiu W, Gossard DC (2010) 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 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
  • 97
    • 81055141475 scopus 로고    scopus 로고
    • Electron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions
    • Liljeroos L, Huiskonen JT, Ora A, Susi P, Butcher SJ (2011) Electron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions. Proc Natl Acad Sci U S A 108:18085-18090
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 18085-18090
    • Liljeroos, L.1    Huiskonen, J.T.2    Ora, A.3    Susi, P.4    Butcher, S.J.5
  • 98
    • 77956006893 scopus 로고    scopus 로고
    • The three-dimensional organization of polyribosomes in intact human cells
    • Brandt F, Carlson LA, Hartl FU, Baumeister W, Grünewald K (2010) The three-dimensional organization of polyribosomes in intact human cells. Mol Cell 39:560-569
    • (2010) Mol Cell , vol.39 , pp. 560-569
    • Brandt, F.1    Carlson, L.A.2    Hartl, F.U.3    Baumeister, W.4    Grünewald, K.5
  • 99
    • 65449162388 scopus 로고    scopus 로고
    • Correlative cryo-light microscopy and cryo-electron tomography: From cellular territories to molecular landscapes
    • Plitzko JM, Rigort A, Leis A (2009) Correlative cryo-light microscopy and cryo-electron tomography: from cellular territories to molecular landscapes. Curr Opin Biotechnol 20:83-89
    • (2009) Curr Opin Biotechnol , vol.20 , pp. 83-89
    • Plitzko, J.M.1    Rigort, A.2    Leis, A.3
  • 100
    • 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 LF, Valentijn JA, Valentijn KM, Koning RI, Koster AJ (2009) Tools for correlative cryo-fluorescence microscopy and cryo-electron tomography applied to whole mitochondria in human endothelial cells. Eur J Cell Biol 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
  • 101
    • 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 JA (2011) Correlated fluorescence and 3D electron microscopy with high sensitivity and spatial precision. J Cell Biol 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
  • 104
    • 83455210803 scopus 로고    scopus 로고
    • Three-dimensional technique on trial
    • Reich ES (2011) Three-dimensional technique on trial. Nature 480:303
    • (2011) Nature , vol.480 , pp. 303
    • Reich, E.S.1
  • 108
    • 84862267369 scopus 로고    scopus 로고
    • Crystallography, evolution, and the structure of viruses
    • Rossmann MG (2012) Crystallography, evolution, and the structure of viruses. J Biol Chem 287:9552-9559
    • (2012) J Biol Chem , vol.287 , pp. 9552-9559
    • Rossmann, M.G.1
  • 110
    • 79960194345 scopus 로고    scopus 로고
    • Insights into the evolution of a complex virus from the crystal structure of vaccinia virus d13
    • Bahar MW, Graham SC, Stuart DI, Grimes JM (2011) Insights into the evolution of a complex virus from the crystal structure of vaccinia virus d13. Structure 19:1011-1020
    • (2011) Structure , vol.19 , pp. 1011-1020
    • Bahar, M.W.1    Graham, S.C.2    Stuart, D.I.3    Grimes, J.M.4
  • 115
    • 34548693442 scopus 로고    scopus 로고
    • Cryo-electron microscopy and three-dimensional reconstructions of hepatitis C virus particles
    • Yu X, Qiao M, Atanasov I, Hu Z, Kato T, Liang TJ, Zhou ZH (2007) Cryo-electron microscopy and three-dimensional reconstructions of hepatitis C virus particles. Virology 367:126-134
    • (2007) Virology , vol.367 , pp. 126-134
    • Yu, X.1    Qiao, M.2    Atanasov, I.3    Hu, Z.4    Kato, T.5    Liang, T.J.6    Zhou, Z.H.7
  • 116
    • 84862171357 scopus 로고    scopus 로고
    • Three-dimensional visualization of forming Hepatitis C virus-like particles by electrontomography
    • Badia-Martinez D, Peralta B, Andrés G, Guerra M, Gil-Carton D, Abrescia NG (2012) Three-dimensional visualization of forming Hepatitis C virus-like particles by electrontomography. Virology 430:120-126
    • (2012) Virology , vol.430 , pp. 120-126
    • Badia-Martinez, D.1    Peralta, B.2    Andrés, G.3    Guerra, M.4    Gil-Carton, D.5    Abrescia, N.G.6
  • 117
    • 77957933124 scopus 로고    scopus 로고
    • Ultrastructural and biophysical characterization of hepatitis C virus particles produced in cell culture
    • Gastaminza P, Dryden KA, Boyd B, Wood MR, Law M, Yeager M, Chisari FV (2010) Ultrastructural and biophysical characterization of hepatitis C virus particles produced in cell culture. J Virol 84:10999-11009
    • (2010) J Virol , vol.84 , pp. 10999-11009
    • Gastaminza, P.1    Dryden, K.A.2    Boyd, B.3    Wood, M.R.4    Law, M.5    Yeager, M.6    Chisari, F.V.7
  • 119
    • 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 MF, King J, Nagayama K, Chiu W (2010) Zernike phase contrast cryo-electron microscopy and tomography for structure determination at nanometer and subnanometer resolutions. Structure 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
  • 120
    • 77957245653 scopus 로고    scopus 로고
    • Preparation of 2D crystals of membrane proteins for high-resolution electron crystallography data collection
    • Abeyrathne PD, Chami M, Pantelic RS, Goldie KN, Stahlberg H (2010) Preparation of 2D crystals of membrane proteins for high-resolution electron crystallography data collection. Methods Enzymol 481:25-43
    • (2010) Methods Enzymol , vol.481 , pp. 25-43
    • Abeyrathne, P.D.1    Chami, M.2    Pantelic, R.S.3    Goldie, K.N.4    Stahlberg, H.5
  • 122
    • 77957236004 scopus 로고    scopus 로고
    • 3D reconstruction from electron micrographs a personal account of its development
    • Derosier D (2010) 3D reconstruction from electron micrographs a personal account of its development. Methods Enzymol 481:1-24
    • (2010) Methods Enzymol , vol.481 , pp. 1-24
    • Derosier, D.1
  • 124
    • 51549087356 scopus 로고    scopus 로고
    • Multi-disciplinary studies of viruses: The role of structure in shaping the questions and answers
    • Johnson JE (2008) Multi-disciplinary studies of viruses: the role of structure in shaping the questions and answers. J Struct Biol 163:246-253
    • (2008) J Struct Biol , vol.163 , pp. 246-253
    • Johnson, J.E.1
  • 125
    • 36949066642 scopus 로고
    • Structure of haemoglobin: A three-dimensional Fourier synthesis at 5.5-A. Resolution, obtained by X-ray analysis
    • Perutz MF, Rossmann MG, Cullis AF, Muirhead H, Will G, North AC (1960) Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5-A. Resolution, obtained by X-ray analysis. Nature 185:416-422
    • (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.6
  • 126
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution
    • Putnam CD, Hammel M, Hura GL, Tainer JA (2007) X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution. Q Rev Biophys 40:191-285
    • (2007) Q Rev Biophys , vol.40 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 129
    • 0030863952 scopus 로고    scopus 로고
    • Noncrystallographic symmetry averaging in phase refinement and extension
    • Vellieux FM, Read RJ (1997) Noncrystallographic symmetry averaging in phase refinement and extension. Methods Enzymol 277:18-53
    • (1997) Methods Enzymol , vol.277 , pp. 18-53
    • Vellieux, F.M.1    Read, R.J.2


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