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Volumn 260, Issue 1, 1996, Pages 85-98

Three-dimensional structure of scaffolding-containing phage P22 procapsids by electron cryo-microscopy

Author keywords

Bacteriophage P22; Electron cryo microscopy; Image processing; Three dimensional structure; Virus assembly

Indexed keywords

CAPSID PROTEIN; STRUCTURAL PROTEIN;

EID: 0030570434     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0383     Document Type: Article
Times cited : (86)

References (61)
  • 2
    • 0025060289 scopus 로고
    • Three-dimensional structures of maturable and abortive capsids of equine herpesvirus 1 from cryo-electron microscopy
    • Baker, T. S., Newcomb, W. W., Booy, F. P., Brown, J. C. & Steven, A. C. (1990). Three-dimensional structures of maturable and abortive capsids of equine herpesvirus 1 from cryo-electron microscopy. J. Virol. 64, 563-573.
    • (1990) J. Virol. , vol.64 , pp. 563-573
    • Baker, T.S.1    Newcomb, W.W.2    Booy, F.P.3    Brown, J.C.4    Steven, A.C.5
  • 3
    • 0026329210 scopus 로고
    • Structures of bovine and human papillomaviruses. Analysis by cryoelectron microscopy and three-dimensional image reconstruction
    • Baker, T. S., Newcomb, W. W., Olson, N. H., Cowsert, L. M., Olson, C. & Brown, J. C. (1991). Structures of bovine and human papillomaviruses. Analysis by cryoelectron microscopy and three-dimensional image reconstruction. Biophys. J. 60, 1445-1456.
    • (1991) Biophys. J. , vol.60 , pp. 1445-1456
    • Baker, T.S.1    Newcomb, W.W.2    Olson, N.H.3    Cowsert, L.M.4    Olson, C.5    Brown, J.C.6
  • 4
    • 0021783271 scopus 로고
    • The DNA translocating vertex of dsDNA bacteriophage
    • Bazinet, C. & King, J. (1985). The DNA translocating vertex of dsDNA bacteriophage. Annu. Rev. Microbiol. 39, 109-129.
    • (1985) Annu. Rev. Microbiol. , vol.39 , pp. 109-129
    • Bazinet, C.1    King, J.2
  • 5
    • 0023682381 scopus 로고
    • Initiation of P22 procapsid assembly in vivo
    • Bazinet, C. & King, J. (1988). Initiation of P22 procapsid assembly in vivo. J. Mol. Biol. 202, 77-86.
    • (1988) J. Mol. Biol. , vol.202 , pp. 77-86
    • Bazinet, C.1    King, J.2
  • 6
    • 0015841378 scopus 로고
    • Mechanism of head assembly and DNA encapsulation in Salmonella phage P22: I. Genes, proteins, structures and DNA maturation
    • Botstein, D., Waddell, C. H. & King, J. (1973). Mechanism of head assembly and DNA encapsulation in Salmonella phage P22: I. Genes, proteins, structures and DNA maturation. J. Mol. Biol. 80, 669-695.
    • (1973) J. Mol. Biol. , vol.80 , pp. 669-695
    • Botstein, D.1    Waddell, C.H.2    King, J.3
  • 7
    • 0026930092 scopus 로고
    • Computer-controlled spot-scan imaging of crotoxin complex crystals with 400 keV electrons at near-atomic resolution
    • Brink, J., Chiu, W. & Dougherty, M. (1991). Computer-controlled spot-scan imaging of crotoxin complex crystals with 400 keV electrons at near-atomic resolution. Ultramicroscopy, 46, 229-240.
    • (1991) Ultramicroscopy , vol.46 , pp. 229-240
    • Brink, J.1    Chiu, W.2    Dougherty, M.3
  • 8
    • 0018791696 scopus 로고
    • Molecular organization of the bacteriophage P22 coat protein shell
    • Casjens, S. (1979). Molecular organization of the bacteriophage P22 coat protein shell. J. Mol. Biol. 131, 1-14.
    • (1979) J. Mol. Biol. , vol.131 , pp. 1-14
    • Casjens, S.1
  • 9
    • 0002107186 scopus 로고
    • Control mechanisms in dsDNA bacteriophage assembly
    • (Calendar, R., ed.), Plenum Press, New York
    • Casjens, S. & Hendrix, R. (1988). Control mechanisms in dsDNA bacteriophage assembly. In The Bacteriophages (Calendar, R., ed.), vol. 1, pp. 15-91, Plenum Press, New York.
    • (1988) The Bacteriophages , vol.1 , pp. 15-91
    • Casjens, S.1    Hendrix, R.2
  • 10
    • 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, 202-224.
    • (1974) J. Supramol. Struct. , vol.2 , pp. 202-224
    • Casjens, S.1    King, J.2
  • 11
    • 0026540521 scopus 로고
    • Cauliflower mosaic virus: A 420 subunit (T = 7), multilayer structure
    • Cheng, R. H., Olson, N. H. & Baker, T. S. (1992). Cauliflower mosaic virus: A 420 subunit (T = 7), multilayer structure. Virology, 186, 655-668.
    • (1992) Virology , vol.186 , pp. 655-668
    • Cheng, R.H.1    Olson, N.H.2    Baker, T.S.3
  • 12
    • 0028847173 scopus 로고
    • Proteolytic and conformational control of virus capsid maturation: The bacteriophage HK97 system
    • Conway, J. F., Duda, R. L., Cheng, N., Hendrix, R. W. & Steven, A. C. (1995). Proteolytic and conformational control of virus capsid maturation: The bacteriophage HK97 system. J. Mol. Biol. 253, 86-99.
    • (1995) J. Mol. Biol. , vol.253 , pp. 86-99
    • Conway, J.F.1    Duda, R.L.2    Cheng, N.3    Hendrix, R.W.4    Steven, A.C.5
  • 13
    • 0015242164 scopus 로고
    • Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther, R. A. (1971). Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs. Phil. Trans. Roy. Soc. Lond. B, 261, 221-230.
    • (1971) Phil. Trans. Roy. Soc. Lond. B , vol.261 , pp. 221-230
    • Crowther, R.A.1
  • 14
    • 0014894609 scopus 로고
    • The reconstruction of a three-dimensional structure from projections and its application to electron microscopy
    • Crowther, R. A., DeRosier, D. J. & Klug, A. (1970). The reconstruction of a three-dimensional structure from projections and its application to electron microscopy. Proc. Roy. Soc. Lond. ser. B, 317, 319-340.
    • (1970) Proc. Roy. Soc. Lond. Ser. B , vol.317 , pp. 319-340
    • Crowther, R.A.1    DeRosier, D.J.2    Klug, A.3
  • 15
    • 0028307177 scopus 로고
    • Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy
    • Crowther, R. A., Kiselev, N. A., Böttcher, B., Berriman, J. A., Borisova, G. P., Ose, V. & Pumpens, P. (1994). Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy. Cell, 77, 943-950.
    • (1994) Cell , vol.77 , pp. 943-950
    • Crowther, R.A.1    Kiselev, N.A.2    Böttcher, B.3    Berriman, J.A.4    Borisova, G.P.5    Ose, V.6    Pumpens, P.7
  • 16
    • 0017892996 scopus 로고
    • Adenovirus type 2 assembly analyzed by reversible cross-linking of labile intermediates
    • D'Halluin, J.-C., Martin, G. R., Torpier, G. & Boulanger, P. A. (1978). Adenovirus type 2 assembly analyzed by reversible cross-linking of labile intermediates. J. Virol. 26, 357-363.
    • (1978) J. Virol. , vol.26 , pp. 357-363
    • D'Halluin, J.-C.1    Martin, G.R.2    Torpier, G.3    Boulanger, P.A.4
  • 17
    • 0027366430 scopus 로고
    • Structural transitions during maturation of bacteriophage lambda capsids
    • Dokland, T. & Murialdo, H. (1993). Structural transitions during maturation of bacteriophage lambda capsids. J. Mol. Biol. 233, 682-694.
    • (1993) J. Mol. Biol. , vol.233 , pp. 682-694
    • Dokland, T.1    Murialdo, H.2
  • 18
    • 0022929708 scopus 로고
    • Improvement in high resolution image quality of radiation-sensitive specimens achieved with reduced spot size of the electron beam
    • Downing, K. H. & Glaeser, R. M. (1986). Improvement in high resolution image quality of radiation-sensitive specimens achieved with reduced spot size of the electron beam. Ultramicroscopy, 20, 269-278.
    • (1986) Ultramicroscopy , vol.20 , pp. 269-278
    • Downing, K.H.1    Glaeser, R.M.2
  • 20
    • 0018932980 scopus 로고
    • DNA packaging by the double-stranded DNA bacteriophages
    • Earnshaw, W. C. & Casjens, S. R. (1980). DNA packaging by the double-stranded DNA bacteriophages. Cell, 21, 319-331.
    • (1980) Cell , vol.21 , pp. 319-331
    • Earnshaw, W.C.1    Casjens, S.R.2
  • 21
    • 0018232414 scopus 로고
    • Structure of phage P22 coat protein aggregates formed in the absence of the scaffolding protein
    • Earnshaw, W. & King, J. (1978). Structure of phage P22 coat protein aggregates formed in the absence of the scaffolding protein. J. Mol. Biol. 126, 721-747.
    • (1978) J. Mol. Biol. , vol.126 , pp. 721-747
    • Earnshaw, W.1    King, J.2
  • 22
    • 0017118828 scopus 로고
    • Assembly of the head of bacteriophage P22: X-ray diffraction from heads, proheads and related structures
    • Earnshaw, W., Casjens, S. & Harrison, S. (1976). Assembly of the head of bacteriophage P22: X-ray diffraction from heads, proheads and related structures. J. Mol. Biol. 104, 387-410.
    • (1976) J. Mol. Biol. , vol.104 , pp. 387-410
    • Earnshaw, W.1    Casjens, S.2    Harrison, S.3
  • 24
    • 0020158116 scopus 로고
    • A proposed structure of the prolate phage T4 prehead core. An electron microscopic study
    • Engel, A., van Driel, R. & Driedonks, R. (1982). A proposed structure of the prolate phage T4 prehead core. An electron microscopic study. J. Ultrastruct. Res. 80, 12-22.
    • (1982) J. Ultrastruct. Res. , vol.80 , pp. 12-22
    • Engel, A.1    Van Driel, R.2    Driedonks, R.3
  • 25
    • 0025770720 scopus 로고
    • Nucleotide sequence of the bacteriophage P22 genes required for DNA packaging
    • Eppler, K., Wyckhoff, E., Goates, J., Parr, R. & Casjens, S. (1991). Nucleotide sequence of the bacteriophage P22 genes required for DNA packaging. Virology, 183, 519-538.
    • (1991) Virology , vol.183 , pp. 519-538
    • Eppler, K.1    Wyckhoff, E.2    Goates, J.3    Parr, R.4    Casjens, S.5
  • 26
    • 0019802812 scopus 로고
    • Computer averaging of electron micrographs of 40S ribosomal subunits
    • Frank, J., Verschoor, A. & Boublik, M. (1981). Computer averaging of electron micrographs of 40S ribosomal subunits. Science, 214, 1353-1355.
    • (1981) Science , vol.214 , pp. 1353-1355
    • Frank, J.1    Verschoor, A.2    Boublik, M.3
  • 27
    • 0019458559 scopus 로고
    • Purification of the coat and scaffolding proteins from procapsids of bacteriophage P22
    • Fuller, M. T. & King, J. (1981). Purification of the coat and scaffolding proteins from procapsids of bacteriophage P22. Virology, 112, 529-547.
    • (1981) Virology , vol.112 , pp. 529-547
    • Fuller, M.T.1    King, J.2
  • 28
    • 0020483095 scopus 로고
    • Assembly in vitro of bacteriophage P22 procapsids from purified coat and scaffolding subunits
    • Fuller, M. T. & King, J. (1982). Assembly in vitro of bacteriophage P22 procapsids from purified coat and scaffolding subunits. J. Mol. Biol. 156, 633-665.
    • (1982) J. Mol. Biol. , vol.156 , pp. 633-665
    • Fuller, M.T.1    King, J.2
  • 29
    • 0023666171 scopus 로고
    • The T = 4 envelope of sindbis virus is organized by interactions with a complementary T = 3 capsid
    • Fuller, S. D. (1987). The T = 4 envelope of sindbis virus is organized by interactions with a complementary T = 3 capsid. Cell, 48, 923-934.
    • (1987) Cell , vol.48 , pp. 923-934
    • Fuller, S.D.1
  • 30
    • 0027320418 scopus 로고
    • Conformational transformations in the protein lattice of phage P22 procapsids
    • Galisteo, M. L. & King, J. (1993). Conformational transformations in the protein lattice of phage P22 procapsids. Biophys. J. 65, 227-235.
    • (1993) Biophys. J. , vol.65 , pp. 227-235
    • Galisteo, M.L.1    King, J.2
  • 32
    • 0028130527 scopus 로고
    • Binding of scaffolding subunits within the P22 procapsid lattice
    • Greene, B. & King, J. (1994). Binding of scaffolding subunits within the P22 procapsid lattice. Virology, 205, 188-197.
    • (1994) Virology , vol.205 , pp. 188-197
    • Greene, B.1    King, J.2
  • 33
    • 0024379303 scopus 로고
    • Adenovirus L1 52-and 55-kilodalton proteins are required for assembly of virions
    • Hasson, T. B., Soloway, P. D., Ornelles, D. A., Doerfler, W. & Shenk, T. (1989). Adenovirus L1 52-and 55-kilodalton proteins are required for assembly of virions. J. Virol. 63, 3612-3621.
    • (1989) J. Virol. , vol.63 , pp. 3612-3621
    • Hasson, T.B.1    Soloway, P.D.2    Ornelles, D.A.3    Doerfler, W.4    Shenk, T.5
  • 34
    • 0026757420 scopus 로고
    • Adenovirus L1 52-and 55-kilodalton proteins are present within assembling virions and colocalize with nuclear structures distinct from replication centers
    • Hasson, T. B., Ornelles, D. A. & Shenk, T. (1992). Adenovirus L1 52-and 55-kilodalton proteins are present within assembling virions and colocalize with nuclear structures distinct from replication centers. J. Virol. 66, 6133-6142.
    • (1992) J. Virol. , vol.66 , pp. 6133-6142
    • Hasson, T.B.1    Ornelles, D.A.2    Shenk, T.3
  • 35
    • 0002410957 scopus 로고
    • The biology of bacteriophage Φ X174
    • (Calendar, R., ed.), Plenum Press, New York
    • Hayashi, M., Aoyama, A., Richardson, D. L., Jr & Hayashi, M. N. (1988). The biology of bacteriophage Φ X174. In The Bacteriophages (Calendar, R., ed.), vol. 2, pp. 1-7, Plenum Press, New York.
    • (1988) The Bacteriophages , vol.2 , pp. 1-7
    • Hayashi, M.1    Aoyama, A.2    Richardson D.L., Jr.3    Hayashi, M.N.4
  • 37
    • 0025297775 scopus 로고
    • Form determination of the heads of bacteriophages
    • Kellenberger, E. (1990). Form determination of the heads of bacteriophages. Eur. J. Biochem. 190, 233-248.
    • (1990) Eur. J. Biochem. , vol.190 , pp. 233-248
    • Kellenberger, E.1
  • 38
    • 0016312775 scopus 로고
    • Catalytic head assembling protein in virus morphogenesis
    • King, J. & Casjens, S. (1974). Catalytic head assembling protein in virus morphogenesis. Nature, 251, 112-119.
    • (1974) Nature , vol.251 , pp. 112-119
    • King, J.1    Casjens, S.2
  • 39
    • 0002608842 scopus 로고    scopus 로고
    • The procapsid to capsid transition in double-stranded DNA bacteriophages
    • (Chiu, W., Burnett, R. M. & Garcea, R. L., eds), Oxford University Press, New York, in the press
    • King, J. & Chiu, W. (1996). The procapsid to capsid transition in double-stranded DNA bacteriophages. In Structural Biology of Viruses (Chiu, W., Burnett, R. M. & Garcea, R. L., eds), Oxford University Press, New York, in the press.
    • (1996) Structural Biology of Viruses
    • King, J.1    Chiu, W.2
  • 40
    • 0015897898 scopus 로고
    • Mechanism of head assembly and DNA encapsulation in Salmonella phage P22. II. Morphogenetic pathway
    • King, J., Lenk, E. V. & Botstein, D. (1973). Mechanism of head assembly and DNA encapsulation in Salmonella phage P22. II. Morphogenetic pathway. J. Mol. Biol. 80, 697-731.
    • (1973) J. Mol. Biol. , vol.80 , pp. 697-731
    • King, J.1    Lenk, E.V.2    Botstein, D.3
  • 41
    • 0029087521 scopus 로고
    • The capsid size-determining protein Sid forms an external scaffold on phage P4 procapsids
    • Marvik, O. J., Dokland, T., Noklin, R. H., Jacobsen, E., Larsen, T. & Lindqvist, B. H. (1995). The capsid size-determining protein Sid forms an external scaffold on phage P4 procapsids. J. Mol. Biol. 251, 59-75.
    • (1995) J. Mol. Biol. , vol.251 , pp. 59-75
    • Marvik, O.J.1    Dokland, T.2    Noklin, R.H.3    Jacobsen, E.4    Larsen, T.5    Lindqvist, B.H.6
  • 42
    • 0026098298 scopus 로고
    • Structure of the herpes simplex virus capsid: Effects of extraction with guanidine hydrochloride and partial reconstitution of extracted capsids
    • Newcomb, W. W. & Brown, J. C. (1991). Structure of the herpes simplex virus capsid: Effects of extraction with guanidine hydrochloride and partial reconstitution of extracted capsids. J. Virol. 65, 613-620.
    • (1991) J. Virol. , vol.65 , pp. 613-620
    • Newcomb, W.W.1    Brown, J.C.2
  • 43
    • 0017572984 scopus 로고
    • Properties of nucleocapsid species isolated from in vivo herpesvirus infection
    • O'Callaghan, D. J., Kemp, M. C. & Randall, C. C. (1977). Properties of nucleocapsid species isolated from in vivo herpesvirus infection. J. Gen. Virol. 37, 585-594.
    • (1977) J. Gen. Virol. , vol.37 , pp. 585-594
    • O'Callaghan, D.J.1    Kemp, M.C.2    Randall, C.C.3
  • 44
    • 0024475524 scopus 로고
    • Magnification calibration and the determination of spherical virus diameters using cryo-microscopy
    • Olson, N. H. & Baker, T. S. (1989). Magnification calibration and the determination of spherical virus diameters using cryo-microscopy. Ultramicroscopy, 30, 281-297.
    • (1989) Ultramicroscopy , vol.30 , pp. 281-297
    • Olson, N.H.1    Baker, T.S.2
  • 45
    • 0017353813 scopus 로고
    • Morphogenetic core of the bacteriophage T4 head. Structure of the core in polyheads
    • Paulson, J. R. & Laemmli, U. K. (1977). Morphogenetic core of the bacteriophage T4 head. Structure of the core in polyheads. J. Mol. Biol. 111, 459-485.
    • (1977) J. Mol. Biol. , vol.111 , pp. 459-485
    • Paulson, J.R.1    Laemmli, U.K.2
  • 46
    • 0018751698 scopus 로고
    • Purification and properties of proteins essential to DNA encapsulation by phage P22
    • Poteete, A. R. & Botstein, D. (1979). Purification and properties of proteins essential to DNA encapsulation by phage P22. Virology, 95, 565-573.
    • (1979) Virology , vol.95 , pp. 565-573
    • Poteete, A.R.1    Botstein, D.2
  • 47
    • 0027278758 scopus 로고
    • Three-dimensional transformation of capsids associated with genome packaging in a bacterial virus
    • Prasad, B. V. V., Prevelige, P. E., Marietta, E., Chen, R. O., Thomas, D., King, J. & Chiu, W. (1993). Three-dimensional transformation of capsids associated with genome packaging in a bacterial virus. J. Mol. Biol. 231, 65-74.
    • (1993) J. Mol. Biol. , vol.231 , pp. 65-74
    • Prasad, B.V.V.1    Prevelige, P.E.2    Marietta, E.3    Chen, R.O.4    Thomas, D.5    King, J.6    Chiu, W.7
  • 48
    • 0027345601 scopus 로고
    • Assembly of bacteriophage P22: A model for ds-DNA virus assembly
    • Prevelige, P. E., Jr & King, J. (1993). Assembly of bacteriophage P22: A model for ds-DNA virus assembly. Prog. Med. Virol. 40, 206-221.
    • (1993) Prog. Med. Virol. , vol.40 , pp. 206-221
    • Prevelige P.E., Jr.1    King, J.2
  • 49
    • 0023696277 scopus 로고
    • Scaffolding protein regulates the polymerization of P22 coat subunits into icosahedral shells in vitro
    • Prevelige, P. E., Jr, Thomas, D. & King, J. (1988). Scaffolding protein regulates the polymerization of P22 coat subunits into icosahedral shells in vitro. J. Mol. Biol. 202, 743-757.
    • (1988) J. Mol. Biol. , vol.202 , pp. 743-757
    • Prevelige P.E., Jr.1    Thomas, D.2    King, J.3
  • 50
    • 0027232759 scopus 로고
    • Nucleation and growth phases in the polymerization of coat and scaffolding subunits into icosahedral procapsid shells
    • Prevelige, P. E., Jr, Thomas, D. & King, J. (1993). Nucleation and growth phases in the polymerization of coat and scaffolding subunits into icosahedral procapsid shells. Biophys. J. 64, 824-835.
    • (1993) Biophys. J. , vol.64 , pp. 824-835
    • Prevelige P.E., Jr.1    Thomas, D.2    King, J.3
  • 51
    • 0001339881 scopus 로고
    • Three-dimensional reconstruction of single particles from random and nonrandom tilt series
    • Radermacher, M. (1988). Three-dimensional reconstruction of single particles from random and nonrandom tilt series. J. Electron Microsc. Tech. 9, 359-394.
    • (1988) J. Electron Microsc. Tech. , vol.9 , pp. 359-394
    • Radermacher, M.1
  • 52
    • 0001315638 scopus 로고
    • Structure and assembly of herpes-viruses
    • Rixon, F. J. (1993). Structure and assembly of herpes-viruses. Semin. Virol. 4, 135-144.
    • (1993) Semin. Virol. , vol.4 , pp. 135-144
    • Rixon, F.J.1
  • 53
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial cell envelope protein
    • Saxton, W. O. & Baumeister, W. (1982). The correlation averaging of a regularly arranged bacterial cell envelope protein. J. Microsc. 127, 127-138.
    • (1982) J. Microsc. , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 54
    • 0026006259 scopus 로고
    • Image reconstruction reveals the complex molecular organization of adenovirus
    • Stewart, P. L., Burnett, R. M., Cyrklaff, M. & Fuller, S. D. (1991). Image reconstruction reveals the complex molecular organization of adenovirus. Cell, 67, 145-154.
    • (1991) Cell , vol.67 , pp. 145-154
    • Stewart, P.L.1    Burnett, R.M.2    Cyrklaff, M.3    Fuller, S.D.4
  • 55
    • 0025726316 scopus 로고
    • A pilot protein participates in the initiation of P22 procapsid assembly
    • Thomas, D. & Prevelige, P., Jr (1991). A pilot protein participates in the initiation of P22 procapsid assembly. Virology, 182, 673-681.
    • (1991) Virology , vol.182 , pp. 673-681
    • Thomas, D.1    Prevelige P., Jr.2
  • 56
    • 0001049902 scopus 로고
    • Automatic detection of spherical particles in close to focus spot-scan electron cryomicroscopy images
    • Thuman-Commike, P. & Chiu, W. (1995). Automatic detection of spherical particles in close to focus spot-scan electron cryomicroscopy images. J. Microsc. Soc. Am. 1, 181-201.
    • (1995) J. Microsc. Soc. Am. , vol.1 , pp. 181-201
    • Thuman-Commike, P.1    Chiu, W.2
  • 57
    • 0029991984 scopus 로고    scopus 로고
    • Script P sign script T sign script O sign script O sign ℒ: A software package for the selection of particles from electron cryomicroscopy spot-scan images
    • Thuman-Commike, P. & Chiu, W. (1996). script P sign script T sign script O sign script O sign ℒ: A software package for the selection of particles from electron cryomicroscopy spot-scan images. J. Struct. Biol. 116, 41-47.
    • (1996) J. Struct. Biol. , vol.116 , pp. 41-47
    • Thuman-Commike, P.1    Chiu, W.2
  • 58
    • 0002573122 scopus 로고
    • Arthropod Hemocyanin structures studied by image analysis
    • In EMBO Workshop: Structure and Function of Invertebrate Respiratory Proteins (Wood, E., ed.), EMBO Workshop, Heidelberg
    • van Heel, M., Keegstra, W., Schutter, W. & van Bruggen, E. (1982). Arthropod Hemocyanin structures studied by image analysis. In EMBO Workshop: Structure and Function of Invertebrate Respiratory Proteins (Wood, E., ed.), Life Chemistry Reports, supplement 1, pp. 69-73, EMBO Workshop, Heidelberg.
    • (1982) Life Chemistry Reports , Issue.SUPPL. 1 , pp. 69-73
    • Van Heel, M.1    Keegstra, W.2    Schutter, W.3    Van Bruggen, E.4
  • 60
    • 0029928874 scopus 로고    scopus 로고
    • CTF determination of images of ice-embedded single particles using a graphics interface
    • Zhou, Z. H., Hardt, S., Wang, B., Sherman, M. B., Jakana, J. & Chiu, W. (1996). CTF determination of images of ice-embedded single particles using a graphics interface. J. Struct. Biol. 116, 216-222.
    • (1996) J. Struct. Biol. , vol.116 , pp. 216-222
    • Zhou, Z.H.1    Hardt, S.2    Wang, B.3    Sherman, M.B.4    Jakana, J.5    Chiu, W.6
  • 61
    • 0028151168 scopus 로고
    • Protein subunit structures in the herpes simplex virus A-capsid determined from 400 kV spot-scan electron cryomicroscopy
    • Zhou, Z. H., Prasad, B. V. V., Jakana, J., Rixon, F. & Chiu, W. (1994). Protein subunit structures in the herpes simplex virus A-capsid determined from 400 kV spot-scan electron cryomicroscopy. J. Mol. Biol. 242, 458-469.
    • (1994) J. Mol. Biol. , vol.242 , pp. 458-469
    • Zhou, Z.H.1    Prasad, B.V.V.2    Jakana, J.3    Rixon, F.4    Chiu, W.5


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