메뉴 건너뛰기




Volumn 11, Issue 3, 2003, Pages 309-322

The receptor binding protein P2 of PRD1, a virus targeting antibiotic-resistant bacteria, has a novel fold suggesting multiple functions

Author keywords

Antibiotic resistance; Bacteriophage PRD1; Receptor binding protein; Tectiviridae; X ray crystallography

Indexed keywords

BACTERIAL PROTEIN; BINDING PROTEIN; MONOMER; PROTEIN P2; UNCLASSIFIED DRUG;

EID: 0037334514     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(03)00023-6     Document Type: Article
Times cited : (40)

References (72)
  • 2
    • 0016287852 scopus 로고
    • Characteristics of PRD1, a plasmid-dependent broad host range DNA bacteriophage
    • Olsen R.H., Siak J.-S., Gray R.H. Characteristics of PRD1, a plasmid-dependent broad host range DNA bacteriophage. J. Virol. 14:1974;689-699.
    • (1974) J. Virol. , vol.14 , pp. 689-699
    • Olsen, R.H.1    Siak, J.-S.2    Gray, R.H.3
  • 3
    • 0036887159 scopus 로고    scopus 로고
    • Sequential model of phage PRD1 DNA delivery: Active involvement of the viral membrane
    • Grahn A.M., Daugelavicius R., Bamford D.H. Sequential model of phage PRD1 DNA delivery. active involvement of the viral membrane Mol. Microbiol. 46:2002;1199-1209.
    • (2002) Mol. Microbiol. , vol.46 , pp. 1199-1209
    • Grahn, A.M.1    Daugelavicius, R.2    Bamford, D.H.3
  • 4
    • 0029159163 scopus 로고
    • Bacteriophage PRD1: A broad host range dsDNA tectivirus with an internal membrane
    • Bamford D.H., Caldentey J., Bamford J.K.H. Bacteriophage PRD1. a broad host range dsDNA tectivirus with an internal membrane Adv. Virus Res. 45:1995;281-319.
    • (1995) Adv. Virus Res. , vol.45 , pp. 281-319
    • Bamford, D.H.1    Caldentey, J.2    Bamford, J.K.H.3
  • 5
    • 0029561893 scopus 로고
    • DNA packaging orders the membrane of bacteriophage PRD1
    • Butcher S.J., Bamford D.H., Fuller S.D. DNA packaging orders the membrane of bacteriophage PRD1. EMBO J. 14:1995;6078-6086.
    • (1995) EMBO J. , vol.14 , pp. 6078-6086
    • Butcher, S.J.1    Bamford, D.H.2    Fuller, S.D.3
  • 6
    • 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
    • San Martín C., 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. 9:2001;917-930.
    • (2001) Structure , vol.9 , pp. 917-930
    • San Martín, 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
  • 7
    • 0019821303 scopus 로고
    • Comparison of the lipid-containing bacteriophages PRD1, PR3, PR4, PR5 and L17
    • Bamford D.H., Rouhiainen L., Takkinen K., Söderlund H. Comparison of the lipid-containing bacteriophages PRD1, PR3, PR4, PR5 and L17. J. Gen. Virol. 57:1981;365-373.
    • (1981) J. Gen. Virol. , vol.57 , pp. 365-373
    • Bamford, D.H.1    Rouhiainen, L.2    Takkinen, K.3    Söderlund, H.4
  • 8
    • 0026006259 scopus 로고
    • Image reconstruction reveals the complex molecular organization of adenovirus
    • Stewart P.L., Burnett R.M., Cyrklaff M., Fuller S.D. Image reconstruction reveals the complex molecular organization of adenovirus. Cell. 67:1991;145-154.
    • (1991) Cell , vol.67 , pp. 145-154
    • Stewart, P.L.1    Burnett, R.M.2    Cyrklaff, M.3    Fuller, S.D.4
  • 9
    • 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. 98:1999;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
  • 10
    • 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 Å resolution
    • Benson S.D., Bamford J.K.H., Bamford D.H., Burnett R.M. The X-ray crystal structure of P3, the major coat protein of the lipid-containing bacteriophage PRD1, at 1.65 Å resolution. Acta Crystallogr. D. 58:2002;39-59.
    • (2002) Acta Crystallogr. D , vol.58 , pp. 39-59
    • Benson, S.D.1    Bamford, J.K.H.2    Bamford, D.H.3    Burnett, R.M.4
  • 11
    • 0033661024 scopus 로고    scopus 로고
    • Type-specific epitope locations revealed by X-ray crystallographic study of adenovirus type 5 hexon
    • Rux J.J., Burnett R.M. Type-specific epitope locations revealed by X-ray crystallographic study of adenovirus type 5 hexon. Mol. Ther. 1:2000;18-30.
    • (2000) Mol. Ther. , vol.1 , pp. 18-30
    • Rux, J.J.1    Burnett, R.M.2
  • 12
    • 0035798386 scopus 로고    scopus 로고
    • A minor capsid protein P30 is essential for bacteriophage PRD1 capsid assembly
    • Rydman P.S., Bamford J.K.H., Bamford D.H. A minor capsid protein P30 is essential for bacteriophage PRD1 capsid assembly. J. Mol. Biol. 313:2001;785-795.
    • (2001) J. Mol. Biol. , vol.313 , pp. 785-795
    • Rydman, P.S.1    Bamford, J.K.H.2    Bamford, D.H.3
  • 14
    • 0022348579 scopus 로고
    • Molecular composition of the adenovirus type 2 virion
    • van Oostrum J., Burnett R.M. Molecular composition of the adenovirus type 2 virion. J. Virol. 56:1985;439-448.
    • (1985) J. Virol. , vol.56 , pp. 439-448
    • Van Oostrum, J.1    Burnett, R.M.2
  • 17
    • 0021092717 scopus 로고
    • Evidence for a repeating cross-β sheet structure in the adenovirus fibre
    • Green N.M., Wrigley N.C., Russell W.C., Martin S.R., McLachlan A.D. Evidence for a repeating cross-β sheet structure in the adenovirus fibre. EMBO J. 2:1983;1357-1365.
    • (1983) EMBO J. , vol.2 , pp. 1357-1365
    • Green, N.M.1    Wrigley, N.C.2    Russell, W.C.3    Martin, S.R.4    McLachlan, A.D.5
  • 19
    • 0033584785 scopus 로고    scopus 로고
    • Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR
    • Bewley M.C., Springer K., Zhang Y.-B., Freimuth P., Flanagan J.M. Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR. Science. 286:1999;1579-1583.
    • (1999) Science , vol.286 , pp. 1579-1583
    • Bewley, M.C.1    Springer, K.2    Zhang, Y.-B.3    Freimuth, P.4    Flanagan, J.M.5
  • 20
    • 0028774724 scopus 로고
    • Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 Å resolution
    • Xia D., Henry L.J., Gerard R.D., Deisenhofer J. Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 Å resolution. Structure. 2:1994;1259-1270.
    • (1994) Structure , vol.2 , pp. 1259-1270
    • Xia, D.1    Henry, L.J.2    Gerard, R.D.3    Deisenhofer, J.4
  • 21
    • 0033613385 scopus 로고    scopus 로고
    • A triple β-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein
    • van Raaij M.J., Mitraki A., Lavigne G., Cusack S. A triple β-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein. Nature. 401:1999;935-938.
    • (1999) Nature , vol.401 , pp. 935-938
    • Van Raaij, M.J.1    Mitraki, A.2    Lavigne, G.3    Cusack, S.4
  • 22
    • 0033881384 scopus 로고    scopus 로고
    • A new mutant class, made by targeted mutagenesis, of phage PRD1 reveals that protein P5 connects the receptor binding protein to the vertex
    • Bamford J.K.H., Bamford D.H. A new mutant class, made by targeted mutagenesis, of phage PRD1 reveals that protein P5 connects the receptor binding protein to the vertex. J. Virol. 74:2000;7781-7786.
    • (2000) J. Virol. , vol.74 , pp. 7781-7786
    • Bamford, J.K.H.1    Bamford, D.H.2
  • 23
    • 0034730067 scopus 로고    scopus 로고
    • Assembly of bacteriophage PRD1 spike complex: Role of the multidomain protein P5
    • Caldentey J., Tuma R., Bamford D.H. Assembly of bacteriophage PRD1 spike complex. role of the multidomain protein P5 Biochemistry. 39:2000;10566-10573.
    • (2000) Biochemistry , vol.39 , pp. 10566-10573
    • Caldentey, J.1    Tuma, R.2    Bamford, D.H.3
  • 24
    • 0032745014 scopus 로고    scopus 로고
    • Stable packaging of phage PRD1 DNA requires adsorption protein P2, which binds to the IncP plasmid-encoded conjugative transfer complex
    • Grahn A.M., Caldentey J., Bamford J.K.H., Bamford D.H. Stable packaging of phage PRD1 DNA requires adsorption protein P2, which binds to the IncP plasmid-encoded conjugative transfer complex. J. Bacteriol. 181:1999;6689-6696.
    • (1999) J. Bacteriol. , vol.181 , pp. 6689-6696
    • Grahn, A.M.1    Caldentey, J.2    Bamford, J.K.H.3    Bamford, D.H.4
  • 26
    • 0019947542 scopus 로고
    • The virion of the lipid-containing bacteriophage PR4
    • Davis T.N., Muller E.D., Cronan J.E. Jr. The virion of the lipid-containing bacteriophage PR4. Virology. 120:1982;287-306.
    • (1982) Virology , vol.120 , pp. 287-306
    • Davis, T.N.1    Muller, E.D.2    Cronan J.E., Jr.3
  • 27
  • 28
    • 0030753669 scopus 로고    scopus 로고
    • Assembly of a functional phage PRD1 receptor depends on 11 genes of the IncP plasmid mating pair formation complex
    • Grahn A.M., Haase J., Lanka E., Bamford D.H. Assembly of a functional phage PRD1 receptor depends on 11 genes of the IncP plasmid mating pair formation complex. J. Bacteriol. 179:1997;4733-4740.
    • (1997) J. Bacteriol. , vol.179 , pp. 4733-4740
    • Grahn, A.M.1    Haase, J.2    Lanka, E.3    Bamford, D.H.4
  • 29
    • 0020436576 scopus 로고
    • Assembly of bacteriophage PRD1: Particle formation with wild-type and mutant viruses
    • Mindich L., Bamford D., McGraw T., Mackenzie G. Assembly of bacteriophage PRD1. particle formation with wild-type and mutant viruses J. Virol. 44:1982;1021-1030.
    • (1982) J. Virol. , vol.44 , pp. 1021-1030
    • Mindich, L.1    Bamford, D.2    McGraw, T.3    Mackenzie, G.4
  • 30
    • 0033794321 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of receptor-binding protein P2 of bacteriophage PRD1
    • Xu L., Butcher S.J., Benson S.D., Bamford D.H., Burnett R.M. Crystallization and preliminary X-ray analysis of receptor-binding protein P2 of bacteriophage PRD1. J. Struct. Biol. 131:2000;159-163.
    • (2000) J. Struct. Biol. , vol.131 , pp. 159-163
    • Xu, L.1    Butcher, S.J.2    Benson, S.D.3    Bamford, D.H.4    Burnett, R.M.5
  • 32
    • 0242558716 scopus 로고    scopus 로고
    • β propellers: Structural rigidity and functional diversity
    • Fülöp V., Jones D.T. β propellers. structural rigidity and functional diversity Curr. Opin. Struct. Biol. 9:1999;715-721.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 715-721
    • Fülöp, V.1    Jones, D.T.2
  • 33
    • 0035664056 scopus 로고    scopus 로고
    • Increasing the hydrophobic interaction between terminal W-motifs enhances the stability of Salmonella typhimurium sialidase. A general strategy for the stabilization of β-propeller protein fold
    • Witarto A.B., Sode K. Increasing the hydrophobic interaction between terminal W-motifs enhances the stability of Salmonella typhimurium sialidase. A general strategy for the stabilization of β-propeller protein fold. Protein Eng. 14:2001;891-896.
    • (2001) Protein Eng. , vol.14 , pp. 891-896
    • Witarto, A.B.1    Sode, K.2
  • 34
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233:1993;123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 36
    • 0030069667 scopus 로고    scopus 로고
    • G protein heterodimers: New structures propel new questions
    • Neer E.J., Smith T.F. G protein heterodimers. new structures propel new questions Cell. 84:1996;175-178.
    • (1996) Cell , vol.84 , pp. 175-178
    • Neer, E.J.1    Smith, T.F.2
  • 37
    • 0032485075 scopus 로고    scopus 로고
    • The 1.7 Å crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller
    • Renault L., Nassar N., Vetter I., Becker J., Klebe C., Roth M., Wittinghofer A. The 1.7 Å crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller. Nature. 392:1998;97-101.
    • (1998) Nature , vol.392 , pp. 97-101
    • Renault, L.1    Nassar, N.2    Vetter, I.3    Becker, J.4    Klebe, C.5    Roth, M.6    Wittinghofer, A.7
  • 40
    • 0034993094 scopus 로고    scopus 로고
    • Protein folds propelled by diversity
    • Paoli M. Protein folds propelled by diversity. Prog. Biophys. Mol. Biol. 76:2001;103-130.
    • (2001) Prog. Biophys. Mol. Biol. , vol.76 , pp. 103-130
    • Paoli, M.1
  • 41
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand
    • Xiong J.-P., Stehle T., Zhang R., Joachimiak A., Frech M., Goodman S.L., Arnaout M.A. Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand. Science. 296:2002;151-155.
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.-P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5    Goodman, S.L.6    Arnaout, M.A.7
  • 42
    • 0026665418 scopus 로고
    • The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor
    • Varghese J.N., McKimm-Breschkin J.L., Caldwell J.B., Kortt A.A., Colman P.M. The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor. Proteins. 14:1992;327-332.
    • (1992) Proteins , vol.14 , pp. 327-332
    • Varghese, J.N.1    McKimm-Breschkin, J.L.2    Caldwell, J.B.3    Kortt, A.A.4    Colman, P.M.5
  • 43
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson M.P. The structure and function of proline-rich regions in proteins. Biochem. J. 297:1994;249-260.
    • (1994) Biochem. J. , vol.297 , pp. 249-260
    • Williamson, M.P.1
  • 44
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay B.K., Williamson M.P., Sudol M. The importance of being proline. the interaction of proline-rich motifs in signaling proteins with their cognate domains FASEB J. 14:2000;231-241.
    • (2000) FASEB J. , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 45
    • 0029146950 scopus 로고
    • Characterization of a novel protein-binding module - The WW domain
    • Sudol M., Chen H.I., Bougeret C., Einbond A., Bork P. Characterization of a novel protein-binding module - the WW domain. FEBS Lett. 369:1995;67-71.
    • (1995) FEBS Lett. , vol.369 , pp. 67-71
    • Sudol, M.1    Chen, H.I.2    Bougeret, C.3    Einbond, A.4    Bork, P.5
  • 46
    • 0028148629 scopus 로고
    • Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
    • Lim W.A., Richards F.M., Fox R.O. Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature. 372:1994;375-379.
    • (1994) Nature , vol.372 , pp. 375-379
    • Lim, W.A.1    Richards, F.M.2    Fox, R.O.3
  • 47
    • 0029775570 scopus 로고    scopus 로고
    • Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide
    • Macias M.J., Hyvönen M., Baraldi E., Schultz J., Sudol M., Saraste M., Oschkinat H. Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. Nature. 382:1996;646-649.
    • (1996) Nature , vol.382 , pp. 646-649
    • Macias, M.J.1    Hyvönen, M.2    Baraldi, E.3    Schultz, J.4    Sudol, M.5    Saraste, M.6    Oschkinat, H.7
  • 48
    • 0031692650 scopus 로고    scopus 로고
    • Left-handed polyproline II helix formation is (very) locally driven
    • Creamer T.P. Left-handed polyproline II helix formation is (very) locally driven. Proteins. 33:1998;218-226.
    • (1998) Proteins , vol.33 , pp. 218-226
    • Creamer, T.P.1
  • 49
    • 0032509175 scopus 로고    scopus 로고
    • Exploiting the basis of proline recognition by SH3 and WW domains: Design of N-substituted inhibitors
    • Nguyen J.T., Turck C.W., Cohen F.E., Zuckermann R.N., Lim W.A. Exploiting the basis of proline recognition by SH3 and WW domains. design of N-substituted inhibitors Science. 282:1998;2088-2092.
    • (1998) Science , vol.282 , pp. 2088-2092
    • Nguyen, J.T.1    Turck, C.W.2    Cohen, F.E.3    Zuckermann, R.N.4    Lim, W.A.5
  • 50
    • 0033057517 scopus 로고    scopus 로고
    • Eukaryotic signalling domain homologues in archaea and bacteria. Ancient ancestry and horizontal gene transfer
    • Ponting C.P., Aravind L., Schultz J., Bork P., Koonin E.V. Eukaryotic signalling domain homologues in archaea and bacteria. Ancient ancestry and horizontal gene transfer. J. Mol. Biol. 289:1999;729-745.
    • (1999) J. Mol. Biol. , vol.289 , pp. 729-745
    • Ponting, C.P.1    Aravind, L.2    Schultz, J.3    Bork, P.4    Koonin, E.V.5
  • 52
    • 0028971135 scopus 로고
    • Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease
    • Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease. J. Virol. 69:1995;6810-6818.
    • (1995) J. Virol. , vol.69 , pp. 6810-6818
    • Huang, M.1    Orenstein, J.M.2    Martin, M.A.3    Freed, E.O.4
  • 54
    • 0034610295 scopus 로고    scopus 로고
    • A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: Implications for filovirus budding
    • Harty R.N., Brown M.E., Wang G., Huibregtse J., Hayes F.P. A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase. implications for filovirus budding Proc. Natl. Acad. Sci. USA. 97:2000;13871-13876.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13871-13876
    • Harty, R.N.1    Brown, M.E.2    Wang, G.3    Huibregtse, J.4    Hayes, F.P.5
  • 56
    • 0036136153 scopus 로고    scopus 로고
    • The lytic enzyme of bacteriophage PRD1 is associated with the viral membrane
    • Rydman P.S., Bamford D.H. The lytic enzyme of bacteriophage PRD1 is associated with the viral membrane. J. Bacteriol. 184:2002;104-110.
    • (2002) J. Bacteriol. , vol.184 , pp. 104-110
    • Rydman, P.S.1    Bamford, D.H.2
  • 57
    • 0028242168 scopus 로고
    • Purification of viruses and macromolecular assemblies for structural investigations using a novel ion exchange method
    • Walin L., Tuma R., Thomas G.J. Jr., Bamford D.H. Purification of viruses and macromolecular assemblies for structural investigations using a novel ion exchange method. Virology. 201:1994;1-7.
    • (1994) Virology , vol.201 , pp. 1-7
    • Walin, L.1    Tuma, R.2    Thomas G.J., Jr.3    Bamford, D.H.4
  • 58
    • 0024475084 scopus 로고
    • Quantitation of the adsorption and penetration stages of bacteriophage φ6 infection
    • Olkkonen V.M., Bamford D.H. Quantitation of the adsorption and penetration stages of bacteriophage φ6 infection. Virology. 171:1989;229-238.
    • (1989) Virology , vol.171 , pp. 229-238
    • Olkkonen, V.M.1    Bamford, D.H.2
  • 59
    • 0032527715 scopus 로고    scopus 로고
    • Reactivity of selenomethionine - Dents in the magic bullet?
    • Smith J.L., Thompson A. Reactivity of selenomethionine - dents in the magic bullet? Structure. 6:1998;815-819.
    • (1998) Structure , vol.6 , pp. 815-819
    • Smith, J.L.1    Thompson, A.2
  • 60
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 61
    • 0028103275 scopus 로고
    • Collaborative Computational Project 4) The CCP4 suite: Programs for protein crystallography
    • CCP4 Collaborative Computational Project 4) The CCP4 suite. programs for protein crystallography Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 62
    • 0030818593 scopus 로고    scopus 로고
    • PHASES-95: A program package for processing and analyzing diffraction data from macromolecules
    • Furey W., Swaminathan S. PHASES-95. a program package for processing and analyzing diffraction data from macromolecules Methods Enzymol. 277:1997;590-620.
    • (1997) Methods Enzymol. , vol.277 , pp. 590-620
    • Furey, W.1    Swaminathan, S.2
  • 64
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement in the multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de la Fortelle E., Bricogne G. Maximum-likelihood heavy-atom parameter refinement in the multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276:1997;472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De la Fortelle, E.1    Bricogne, G.2
  • 65
    • 0030855279 scopus 로고    scopus 로고
    • Bias reduction in phase refinement by modified interference functions: Introducing the γ correction
    • Abrahams J.P. Bias reduction in phase refinement by modified interference functions. introducing the γ correction Acta Crystallogr. D. 53:1997;371-376.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 371-376
    • Abrahams, J.P.1
  • 66
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 68
    • 0027609916 scopus 로고
    • Setor: Hardware-lighted three-dimensional solid model representations of macromolecules
    • Evans S.V. Setor. hardware-lighted three-dimensional solid model representations of macromolecules J. Mol. Graph. 11:1993;134-138.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 69
    • 0027412196 scopus 로고
    • Alscript: A tool to format multiple sequence alignments
    • Barton G.J. Alscript. a tool to format multiple sequence alignments Protein Eng. 6:1993;37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 70
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins. 11:1991;281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 71
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. Molscript. a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 72
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphics
    • Merritt E.A., Murphy M.E.P. Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D. 50:1994;869-873.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.