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Volumn 111, Issue 43, 2014, Pages E4606-E4614

Capsid expansion mechanism of bacteriophage T7 revealed by multistate atomic models derived from cryo-EM reconstructions

Author keywords

Bacteriophage T7 maturation; DNA packaging intermediates; Noncovalent topological linking; Procapsid; Single particle cryo EM

Indexed keywords

CAPSID PROTEIN; GENOMIC DNA; SCAFFOLD PROTEIN; PROTEIN BINDING;

EID: 84908434273     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1407020111     Document Type: Article
Times cited : (78)

References (68)
  • 1
    • 79952163890 scopus 로고    scopus 로고
    • Structural basis for scaffolding-mediated assembly and maturation of a dsDNA virus
    • Chen DH, et al. (2011) Structural basis for scaffolding-mediated assembly and maturation of a dsDNA virus. Proc Natl Acad Sci USA 108(4):1355-1360.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.4 , pp. 1355-1360
    • Chen, D.H.1
  • 2
    • 78650939540 scopus 로고    scopus 로고
    • Molecular rearrangements involved in the capsid shell maturation of bacteriophage T7
    • Ionel A, et al. (2011) Molecular rearrangements involved in the capsid shell maturation of bacteriophage T7. J Biol Chem 286(1):234-242.
    • (2011) J Biol Chem , vol.286 , Issue.1 , pp. 234-242
    • Ionel, A.1
  • 3
    • 0037313264 scopus 로고    scopus 로고
    • Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions
    • Jiang W, et al. (2003) Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Nat Struct Biol 10(2):131-135.
    • (2003) Nat Struct Biol , vol.10 , Issue.2 , pp. 131-135
    • Jiang, W.1
  • 4
    • 0042827209 scopus 로고    scopus 로고
    • Molecular mechanisms in bacteriophage T7 procapsid assembly, maturation, and DNA containment
    • Cerritelli ME, Conway JF, Cheng N, Trus BL, Steven AC (2003) Molecular mechanisms in bacteriophage T7 procapsid assembly, maturation, and DNA containment. Adv Protein Chem 64:301-323.
    • (2003) Adv Protein Chem , vol.64 , pp. 301-323
    • Cerritelli, M.E.1    Conway, J.F.2    Cheng, N.3    Trus, B.L.4    Steven, A.C.5
  • 5
    • 0035957688 scopus 로고    scopus 로고
    • Virus maturation involving large subunit rotations and local refolding
    • Conway JF, et al. (2001) Virus maturation involving large subunit rotations and local refolding. Science 292(5517):744-748.
    • (2001) Science , vol.292 , Issue.5517 , pp. 744-748
    • Conway, J.F.1
  • 6
    • 0032582665 scopus 로고    scopus 로고
    • Assembly of a tailed bacterial virus and its genome release studied in three dimensions
    • Tao Y, et al. (1998) Assembly of a tailed bacterial virus and its genome release studied in three dimensions. Cell 95(3):431-437.
    • (1998) Cell , vol.95 , Issue.3 , pp. 431-437
    • Tao, Y.1
  • 7
    • 84893751482 scopus 로고    scopus 로고
    • Architecture of a dsDNA viral capsid in complex with its maturation protease
    • Veesler D, et al. (2014) Architecture of a dsDNA viral capsid in complex with its maturation protease. Structure 22(2):230-237.
    • (2014) Structure , vol.22 , Issue.2 , pp. 230-237
    • Veesler, D.1
  • 8
    • 63849128084 scopus 로고    scopus 로고
    • An unexpected twist in viral capsid maturation
    • Gertsman I, et al. (2009) An unexpected twist in viral capsid maturation. Nature 458(7238):646-650.
    • (2009) Nature , vol.458 , Issue.7238 , pp. 646-650
    • Gertsman, I.1
  • 9
    • 33846262040 scopus 로고    scopus 로고
    • Capsid conformational sampling in HK97 maturation visualized by X-ray crystallography and cryo-EM
    • Gan L, et al. (2006) Capsid conformational sampling in HK97 maturation visualized by X-ray crystallography and cryo-EM. Structure 14(11):1655-1665.
    • (2006) Structure , vol.14 , Issue.11 , pp. 1655-1665
    • Gan, L.1
  • 10
    • 0021770314 scopus 로고
    • Nucleotide sequence of the gene for bacteriophage T7 RNA polymerase
    • Moffatt BA, Dunn JJ, Studier FW (1984) Nucleotide sequence of the gene for bacteriophage T7 RNA polymerase. J Mol Biol 173(2):265-269.
    • (1984) J Mol Biol , vol.173 , Issue.2 , pp. 265-269
    • Moffatt, B.A.1    Dunn, J.J.2    Studier, F.W.3
  • 11
    • 0002059514 scopus 로고    scopus 로고
    • T7Select Phage Display System: A powerful new protein display system based on bacteriophage T7
    • Rosenberg A, et al. (1996) T7Select Phage Display System: A powerful new protein display system based on bacteriophage T7. Innovations 6:1-6.
    • (1996) Innovations , vol.6 , pp. 1-6
    • Rosenberg, A.1
  • 12
    • 0020964297 scopus 로고
    • Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements
    • Dunn JJ, Studier FW (1983) Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements. J Mol Biol 166(4):477-535.
    • (1983) J Mol Biol , vol.166 , Issue.4 , pp. 477-535
    • Dunn, J.J.1    Studier, F.W.2
  • 13
    • 80051788970 scopus 로고    scopus 로고
    • Bacteriophage-host interactions leading to genome internalization
    • Bertin A, de Frutos M, Letellier L (2011) Bacteriophage-host interactions leading to genome internalization. Curr Opin Microbiol 14(4):492-496.
    • (2011) Curr Opin Microbiol , vol.14 , Issue.4 , pp. 492-496
    • Bertin, A.1    De Frutos, M.2    Letellier, L.3
  • 14
    • 34147110201 scopus 로고    scopus 로고
    • Quasi-atomic model of bacteriophage t7 procapsid shell: Insights into the structure and evolution of a basic fold
    • Agirrezabala X, et al. (2007) Quasi-atomic model of bacteriophage t7 procapsid shell: Insights into the structure and evolution of a basic fold. Structure 15(4):461-472.
    • (2007) Structure , vol.15 , Issue.4 , pp. 461-472
    • Agirrezabala, X.1
  • 15
    • 0029998659 scopus 로고    scopus 로고
    • Assembly of T7 capsids from independently expressed and purified head protein and scaffolding protein
    • Cerritelli ME, Studier FW (1996) Assembly of T7 capsids from independently expressed and purified head protein and scaffolding protein. J Mol Biol 258(2):286-298.
    • (1996) J Mol Biol , vol.258 , Issue.2 , pp. 286-298
    • Cerritelli, M.E.1    Studier, F.W.2
  • 16
    • 0018837780 scopus 로고
    • A metrizamide-impermeable capsid in the DNA packaging pathway of bacteriophage T7
    • Serwer P (1980) A metrizamide-impermeable capsid in the DNA packaging pathway of bacteriophage T7. J Mol Biol 138(1):65-91.
    • (1980) J Mol Biol , vol.138 , Issue.1 , pp. 65-91
    • Serwer, P.1
  • 17
    • 0016611256 scopus 로고
    • Buoyant density sedimentation of macromolecules in sodium iothalamate density gradients
    • Serwer P (1975) Buoyant density sedimentation of macromolecules in sodium iothalamate density gradients. J Mol Biol 92(3):433-448.
    • (1975) J Mol Biol , vol.92 , Issue.3 , pp. 433-448
    • Serwer, P.1
  • 18
    • 84876817617 scopus 로고    scopus 로고
    • Visualization of uncorrelated, tandem symmetry mismatches in the internal genome packaging apparatus of bacteriophage T7
    • Guo F, et al. (2013) Visualization of uncorrelated, tandem symmetry mismatches in the internal genome packaging apparatus of bacteriophage T7. Proc Natl Acad Sci USA 110(17):6811-6816.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.17 , pp. 6811-6816
    • Guo, F.1
  • 19
    • 0031218420 scopus 로고    scopus 로고
    • Phage DNA packaging
    • Fujisawa H, Morita M (1997) Phage DNA packaging. Genes Cells 2(9):537-545.
    • (1997) Genes Cells , vol.2 , Issue.9 , pp. 537-545
    • Fujisawa, H.1    Morita, M.2
  • 20
    • 0021840571 scopus 로고
    • The use of polylysine during negative staining of viral suspensions
    • Barth OM (1985) The use of polylysine during negative staining of viral suspensions. J Virol Methods 11(1):23-27.
    • (1985) J Virol Methods , vol.11 , Issue.1 , pp. 23-27
    • Barth, O.M.1
  • 21
    • 84934443131 scopus 로고    scopus 로고
    • Single particle cryo-electron microscopy and 3-D reconstruction of viruses
    • Guo F, Jiang W (2014) Single particle cryo-electron microscopy and 3-D reconstruction of viruses. Methods Mol Biol 1117:401-443.
    • (2014) Methods Mol Biol , vol.1117 , pp. 401-443
    • Guo, F.1    Jiang, W.2
  • 22
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-EM structure determination
    • Scheres SH, Chen S (2012) Prevention of overfitting in cryo-EM structure determination. Nat Methods 9(9):853-854.
    • (2012) Nat Methods , vol.9 , Issue.9 , pp. 853-854
    • Scheres, S.H.1    Chen, S.2
  • 23
    • 84863011711 scopus 로고    scopus 로고
    • Outcome of the first electron microscopy validation task force meeting
    • Henderson R, et al. (2012) Outcome of the first electron microscopy validation task force meeting. Structure 20(2):205-214.
    • (2012) Structure , vol.20 , Issue.2 , pp. 205-214
    • Henderson, R.1
  • 24
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal PB, Henderson R (2003) Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J Mol Biol 333(4):721-745.
    • (2003) J Mol Biol , vol.333 , Issue.4 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 25
    • 42949089487 scopus 로고    scopus 로고
    • Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics
    • Trabuco LG, Villa E, Mitra K, Frank J, Schulten K (2008) Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics. Structure 16(5):673-683.
    • (2008) Structure , vol.16 , Issue.5 , pp. 673-683
    • Trabuco, L.G.1    Villa, E.2    Mitra, K.3    Frank, J.4    Schulten, K.5
  • 26
    • 84879546904 scopus 로고    scopus 로고
    • Structure of the archaeal head-tailed virus HSTV-1 completes the HK97 fold story
    • Pietilä MK, et al. (2013) Structure of the archaeal head-tailed virus HSTV-1 completes the HK97 fold story. Proc Natl Acad Sci USA 110(26):10604-10609.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.26 , pp. 10604-10609
    • Pietilä, M.K.1
  • 27
    • 84880659509 scopus 로고    scopus 로고
    • Validated near-atomic resolution structure of bacteriophage epsilon15 derived from cryo-EM and modeling
    • Baker ML, et al. (2013) Validated near-atomic resolution structure of bacteriophage epsilon15 derived from cryo-EM and modeling. Proc Natl Acad Sci USA 110(30):12301-6.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.30 , pp. 12301-12306
    • Baker, M.L.1
  • 28
    • 0344010492 scopus 로고    scopus 로고
    • The refined structure of a protein catenane: The HK97 bacteriophage capsid at 3.44 A resolution
    • Helgstrand C, et al. (2003) The refined structure of a protein catenane: The HK97 bacteriophage capsid at 3.44 A resolution. J Mol Biol 334(5):885-899.
    • (2003) J Mol Biol , vol.334 , Issue.5 , pp. 885-899
    • Helgstrand, C.1
  • 29
    • 0034703226 scopus 로고    scopus 로고
    • Topologically linked protein rings in the bacteriophage HK97 capsid
    • Wikoff WR, et al. (2000) Topologically linked protein rings in the bacteriophage HK97 capsid. Science 289(5487):2129-2133.
    • (2000) Science , vol.289 , Issue.5487 , pp. 2129-2133
    • Wikoff, W.R.1
  • 30
    • 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(23):14967-14970.
    • (2005) J Virol , vol.79 , Issue.23 , pp. 14967-14970
    • Baker, M.L.1    Jiang, W.2    Rixon, F.J.3    Chiu, W.4
  • 31
    • 79953887810 scopus 로고    scopus 로고
    • The Prohead-I structure of bacteriophage HK97: Implications for scaffold-mediated control of particle assembly and maturation
    • Huang RK, et al. (2011) The Prohead-I structure of bacteriophage HK97: Implications for scaffold-mediated control of particle assembly and maturation. J Mol Biol 408(3):541-554.
    • (2011) J Mol Biol , vol.408 , Issue.3 , pp. 541-554
    • Huang, R.K.1
  • 32
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 33
    • 80055069768 scopus 로고    scopus 로고
    • Decoding bacteriophage P22 assembly: Identification of two charged residues in scaffolding protein responsible for coat protein interaction
    • Cortines JR, Weigele PR, Gilcrease EB, Casjens SR, Teschke CM (2011) Decoding bacteriophage P22 assembly: Identification of two charged residues in scaffolding protein responsible for coat protein interaction. Virology 421(1):1-11.
    • (2011) Virology , vol.421 , Issue.1 , pp. 1-11
    • Cortines, J.R.1    Weigele, P.R.2    Gilcrease, E.B.3    Casjens, S.R.4    Teschke, C.M.5
  • 34
    • 0038419606 scopus 로고    scopus 로고
    • Bacteriophage phi29 scaffolding protein gp7 before and after prohead assembly
    • Morais MC, et al. (2003) Bacteriophage phi29 scaffolding protein gp7 before and after prohead assembly. Nat Struct Biol 10(7):572-576.
    • (2003) Nat Struct Biol , vol.10 , Issue.7 , pp. 572-576
    • Morais, M.C.1
  • 35
    • 0034646575 scopus 로고    scopus 로고
    • Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded DNA virus
    • Sun Y, et al. (2000) Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded DNA virus. J Mol Biol 297(5):1195-1202.
    • (2000) J Mol Biol , vol.297 , Issue.5 , pp. 1195-1202
    • Sun, Y.1
  • 36
    • 0017102281 scopus 로고
    • Internal proteins of bacteriophage T7
    • Serwer P (1976) Internal proteins of bacteriophage T7. J Mol Biol 107(3):271-291.
    • (1976) J Mol Biol , vol.107 , Issue.3 , pp. 271-291
    • Serwer, P.1
  • 37
    • 84890467275 scopus 로고    scopus 로고
    • A new topology of the HK97-like fold revealed in Bordetella bacteriophage by cryoEM at 3.5 A resolution
    • Zhang X, et al. (2013) A new topology of the HK97-like fold revealed in Bordetella bacteriophage by cryoEM at 3.5 A resolution. eLife 2:e01299.
    • (2013) eLife , vol.2 , pp. e01299
    • Zhang, X.1
  • 38
    • 84902155565 scopus 로고    scopus 로고
    • Single-step antibody-based affinity cryo-electron microscopy for imaging and structural analysis of macromolecular assemblies
    • Yu G, et al. (2014) Single-step antibody-based affinity cryo-electron microscopy for imaging and structural analysis of macromolecular assemblies. J Struct Biol 187(1):1-9.
    • (2014) J Struct Biol , vol.187 , Issue.1 , pp. 1-9
    • Yu, G.1
  • 39
    • 0031606857 scopus 로고    scopus 로고
    • Bacteriophage HK97 head assembly: A protein ballet
    • Hendrix RW, Duda RL (1998) Bacteriophage HK97 head assembly: A protein ballet. Adv Virus Res 50:235-288.
    • (1998) Adv Virus Res , vol.50 , pp. 235-288
    • Hendrix, R.W.1    Duda, R.L.2
  • 40
    • 0016370643 scopus 로고
    • P22 morphogenesis. I: Catalytic scaffolding protein in capsid assembly
    • Casjens S, King J (1974) P22 morphogenesis. I: Catalytic scaffolding protein in capsid assembly. J Supramol Struct 2(2-4):202-224.
    • (1974) J Supramol Struct , vol.2 , Issue.2-4 , pp. 202-224
    • Casjens, S.1    King, J.2
  • 41
    • 0025908787 scopus 로고
    • The maturation-dependent conformational change of phage T4 capsid involves the translocation of specific epitopes between the inner and the outer capsid surfaces
    • Steven AC, Bauer AC, Bisher ME, Robey FA, Black LW (1991) The maturation-dependent conformational change of phage T4 capsid involves the translocation of specific epitopes between the inner and the outer capsid surfaces. J Struct Biol 106(3):221-236.
    • (1991) J Struct Biol , vol.106 , Issue.3 , pp. 221-236
    • Steven, A.C.1    Bauer, A.C.2    Bisher, M.E.3    Robey, F.A.4    Black, L.W.5
  • 42
    • 33750712806 scopus 로고    scopus 로고
    • Adeno-associated virus type 2 capsids with externalized VP1/VP2 trafficking domains are generated prior to passage through the cytoplasm and are maintained until uncoating occurs in the nucleus
    • Sonntag F, Bleker S, Leuchs B, Fischer R, Kleinschmidt JA (2006) Adeno-associated virus type 2 capsids with externalized VP1/VP2 trafficking domains are generated prior to passage through the cytoplasm and are maintained until uncoating occurs in the nucleus. J Virol 80(22):11040-11054.
    • (2006) J Virol , vol.80 , Issue.22 , pp. 11040-11054
    • Sonntag, F.1    Bleker, S.2    Leuchs, B.3    Fischer, R.4    Kleinschmidt, J.A.5
  • 43
    • 17444405970 scopus 로고    scopus 로고
    • A conformational change in the adeno-associated virus type 2 capsid leads to the exposure of hidden VP1 N termini
    • Kronenberg S, Böttcher B, von der Lieth CW, Bleker S, Kleinschmidt JA (2005) A conformational change in the adeno-associated virus type 2 capsid leads to the exposure of hidden VP1 N termini. J Virol 79(9):5296-5303.
    • (2005) J Virol , vol.79 , Issue.9 , pp. 5296-5303
    • Kronenberg, S.1    Böttcher, B.2    Von Der Lieth, C.W.3    Bleker, S.4    Kleinschmidt, J.A.5
  • 44
    • 0035159863 scopus 로고    scopus 로고
    • The N-terminal region of the VP1 protein of swine vesicular disease virus contains a neutralization site that arises upon cell attachment and is involved in viral entry
    • Jiménez-Clavero MA, Escribano-Romero E, Douglas AJ, Ley V (2001) The N-terminal region of the VP1 protein of swine vesicular disease virus contains a neutralization site that arises upon cell attachment and is involved in viral entry. J Virol 75(2):1044-1047.
    • (2001) J Virol , vol.75 , Issue.2 , pp. 1044-1047
    • Jiménez-Clavero, M.A.1    Escribano-Romero, E.2    Douglas, A.J.3    Ley, V.4
  • 45
    • 73649087232 scopus 로고    scopus 로고
    • Structure of the small outer capsid protein, Soc: A clamp for stabilizing capsids of T4-like phages
    • Qin L, Fokine A, O' Donnell E, Rao VB, Rossmann MG (2010) Structure of the small outer capsid protein, Soc: A clamp for stabilizing capsids of T4-like phages. J Mol Biol 395(4):728-741.
    • (2010) J Mol Biol , vol.395 , Issue.4 , pp. 728-741
    • Qin, L.1    Fokine, A.2    O'Donnell, E.3    Rao, V.B.4    Rossmann, M.G.5
  • 46
    • 1942533523 scopus 로고    scopus 로고
    • Molecular architecture of the prolate head of bacteriophage T4
    • Fokine A, et al. (2004) Molecular architecture of the prolate head of bacteriophage T4. Proc Natl Acad Sci USA 101(16):6003-6008.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.16 , pp. 6003-6008
    • Fokine, A.1
  • 47
    • 50849118817 scopus 로고    scopus 로고
    • Bacteriophage lambda stabilization by auxiliary protein gpD: Timing, location, and mechanism of attachment determined by cryo-EM
    • Lander GC, et al. (2008) Bacteriophage lambda stabilization by auxiliary protein gpD: Timing, location, and mechanism of attachment determined by cryo-EM. Structure 16(9):1399-1406.
    • (2008) Structure , vol.16 , Issue.9 , pp. 1399-1406
    • Lander, G.C.1
  • 48
    • 84927693101 scopus 로고    scopus 로고
    • Bacteria-phage coevolution as a driver of ecological and evolutionary processes in microbial communities
    • Koskella B, Brockhurst MA (2014) Bacteria-phage coevolution as a driver of ecological and evolutionary processes in microbial communities. FEMS Microbiol Rev 38(5):916-931.
    • (2014) FEMS Microbiol Rev , vol.38 , Issue.5 , pp. 916-931
    • Koskella, B.1    Brockhurst, M.A.2
  • 49
    • 36048971347 scopus 로고    scopus 로고
    • The genome of epsilon15, a serotype-converting, Group E1 Salmonella enterica-specific bacteriophage
    • Kropinski AM, et al. (2007) The genome of epsilon15, a serotype-converting, Group E1 Salmonella enterica-specific bacteriophage. Virology 369(2):234-244.
    • (2007) Virology , vol.369 , Issue.2 , pp. 234-244
    • Kropinski, A.M.1
  • 50
    • 0037335488 scopus 로고    scopus 로고
    • Bacteriophage T4 genome
    • Miller ES, et al. (2003) Bacteriophage T4 genome. Microbiol Mol Biol Rev 67(1):86-156.
    • (2003) Microbiol Mol Biol Rev , vol.67 , Issue.1 , pp. 86-156
    • Miller, E.S.1
  • 51
    • 0033754089 scopus 로고    scopus 로고
    • Sequence of the genome of Salmonella bacteriophage P22
    • Vander Byl C, Kropinski AM (2000) Sequence of the genome of Salmonella bacteriophage P22. J Bacteriol 182(22):6472-6481.
    • (2000) J Bacteriol , vol.182 , Issue.22 , pp. 6472-6481
    • Vander Byl, C.1    Kropinski, A.M.2
  • 52
    • 0034716946 scopus 로고    scopus 로고
    • Genomic sequences of bacteriophages HK97 and HK022: Pervasive genetic mosaicism in the lambdoid bacteriophages
    • Juhala RJ, et al. (2000) Genomic sequences of bacteriophages HK97 and HK022: Pervasive genetic mosaicism in the lambdoid bacteriophages. J Mol Biol 299(1):27-51.
    • (2000) J Mol Biol , vol.299 , Issue.1 , pp. 27-51
    • Juhala, R.J.1
  • 54
    • 0034034401 scopus 로고    scopus 로고
    • Biological significance of a family of regularly spaced repeats in the genomes of Archaea, Bacteria and mitochondria
    • Mojica FJ, Díez-Villaseñor C, Soria E, Juez G (2000) Biological significance of a family of regularly spaced repeats in the genomes of Archaea, Bacteria and mitochondria. Mol Microbiol 36(1):244-246.
    • (2000) Mol Microbiol , vol.36 , Issue.1 , pp. 244-246
    • Mojica, F.J.1    Díez-Villaseñor, C.2    Soria, E.3    Juez, G.4
  • 55
    • 67650697753 scopus 로고    scopus 로고
    • Structure and energetics of encapsidated DNA in bacteriophage HK97 studied by scanning calorimetry and cryo-electron microscopy
    • Duda RL, et al. (2009) Structure and energetics of encapsidated DNA in bacteriophage HK97 studied by scanning calorimetry and cryo-electron microscopy. J Mol Biol 391(2):471-483.
    • (2009) J Mol Biol , vol.391 , Issue.2 , pp. 471-483
    • Duda, R.L.1
  • 56
    • 33746931256 scopus 로고    scopus 로고
    • Bacteriophage T5 structure reveals similarities with HK97 and T4 suggesting evolutionary relationships
    • Effantin G, Boulanger P, Neumann E, Letellier L, Conway JF (2006) Bacteriophage T5 structure reveals similarities with HK97 and T4 suggesting evolutionary relationships. J Mol Biol 361(5):993-1002.
    • (2006) J Mol Biol , vol.361 , Issue.5 , pp. 993-1002
    • Effantin, G.1    Boulanger, P.2    Neumann, E.3    Letellier, L.4    Conway, J.F.5
  • 57
    • 0035909370 scopus 로고    scopus 로고
    • The bacteriophage straight phi29 portal motor can package DNA against a large internal force
    • Smith DE, et al. (2001) The bacteriophage straight phi29 portal motor can package DNA against a large internal force. Nature 413(6857):748-752.
    • (2001) Nature , vol.413 , Issue.6857 , pp. 748-752
    • Smith, D.E.1
  • 58
    • 0033787642 scopus 로고    scopus 로고
    • Local average intensity-based method for identifying spherical particles in electron micrographs
    • Kivioja T, Ravantti J, Verkhovsky A, Ukkonen E, Bamford D (2000) Local average intensity-based method for identifying spherical particles in electron micrographs. J Struct Biol 131(2):126-134.
    • (2000) J Struct Biol , vol.131 , Issue.2 , pp. 126-134
    • Kivioja, T.1    Ravantti, J.2    Verkhovsky, A.3    Ukkonen, E.4    Bamford, D.5
  • 59
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: Semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 128(1):82-97.
    • (1999) J Struct Biol , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 60
    • 84867904359 scopus 로고    scopus 로고
    • A graph theory method for determination of cryo-EM image focuses
    • Jiang W, Guo F, Liu Z (2012) A graph theory method for determination of cryo-EM image focuses. J Struct Biol 180(2):343-351.
    • (2012) J Struct Biol , vol.180 , Issue.2 , pp. 343-351
    • Jiang, W.1    Guo, F.2    Liu, Z.3
  • 61
    • 61449100438 scopus 로고    scopus 로고
    • Estimating contrast transfer function and associated parameters by constrained non-linear optimization
    • Yang C, et al. (2009) Estimating contrast transfer function and associated parameters by constrained non-linear optimization. J Microsc 233(3):391-403.
    • (2009) J Microsc , vol.233 , Issue.3 , pp. 391-403
    • Yang, C.1
  • 62
    • 33845348934 scopus 로고    scopus 로고
    • Ab initio random model method facilitates 3D reconstruction of icosahedral particles
    • Yan X, Dryden KA, Tang J, Baker TS (2007) Ab initio random model method facilitates 3D reconstruction of icosahedral particles. J Struct Biol 157(1):211-225.
    • (2007) J Struct Biol , vol.157 , Issue.1 , pp. 211-225
    • Yan, X.1    Dryden, K.A.2    Tang, J.3    Baker, T.S.4
  • 63
    • 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 (2007) 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 160(1):11-27.
    • (2007) J Struct Biol , vol.160 , Issue.1 , pp. 11-27
    • Liu, X.1    Jiang, W.2    Jakana, J.3    Chiu, W.4
  • 64
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • Tang G, et al. (2007) EMAN2: An extensible image processing suite for electron microscopy. J Struct Biol 157(1):38-46.
    • (2007) J Struct Biol , vol.157 , Issue.1 , pp. 38-46
    • Tang, G.1
  • 65
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Pt 1
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 66
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera - a visualization system for exploratory research and analysis. J Comput Chem 25(13):1605-1612.
    • (2004) J Comput Chem , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1
  • 67
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50(Pt 5):760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 68
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen VB, et al. (2010) MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66(Pt 1):12-21.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 12-21
    • Chen, V.B.1


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