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Volumn 6, Issue 5, 1999, Pages 458-463

Automated protein model building combined with iterative structure refinement

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; AUTOMATION; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

EID: 0032964481     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/8263     Document Type: Article
Times cited : (2583)

References (17)
  • 1
    • 0017411710 scopus 로고
    • The Protein Data Bank: A computer-based archival file for macromolecular structures
    • Bernstein, F.C. et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542 (1977).
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Bernstein, F.C.1
  • 2
    • 0031879551 scopus 로고    scopus 로고
    • Synchrotron radiation facilities
    • Helliwell, J.R. Synchrotron radiation facilities. Nature Struct. Biol. 5, 614-617 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 614-617
    • Helliwell, J.R.1
  • 3
    • 0031903288 scopus 로고    scopus 로고
    • MAD phasing grows up
    • Ogata, CM. MAD phasing grows up. Nature Struct. Biol. 5, 633-640 (1998)
    • (1998) Nature Struct. Biol. , vol.5 , pp. 633-640
    • Ogata, C.M.1
  • 4
    • 0030818593 scopus 로고    scopus 로고
    • PHASES-95: A program package for the processing and analyzing diffraction data from macromolecules
    • Furey, W. & Swaminathan, S. PHASES-95: a program package for the processing and analyzing diffraction data from macromolecules. Methods Enzymol. 277, 590-620 (1997).
    • (1997) Methods Enzymol. , vol.277 , pp. 590-620
    • Furey, W.1    Swaminathan, S.2
  • 6
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • Fortelle de La, E. & Bricogne, G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 590-620 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 590-620
    • Fortelle De La, E.1    Bricogne, G.2
  • 7
    • 0033119895 scopus 로고    scopus 로고
    • Automated structure solution for MIR and MAD
    • Terwilliger, T.C. & Berendzen, J. Automated structure solution for MIR and MAD. Acta Crystallogr. D 55, 849-861 (1999).
    • (1999) Acta Crystallogr. D , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 8
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR System: A new software suite for macromolecular structure determination
    • Brünger, A.T. et al. Crystallography & NMR System: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 9
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 11
    • 0031045587 scopus 로고    scopus 로고
    • Patterson superposition and ab initio phasing
    • Sheldrick, G.M. Patterson superposition and ab initio phasing. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Sheldrick, G.M.1
  • 12
    • 0032168975 scopus 로고    scopus 로고
    • On the ab Initio solution of the phase problem for macromolecules at very low resolution. II. Generalized likelihood based approach to cluster discrimination
    • Lunin, V.Y., Lunina, N.L., Petrova, T.E., Urzhumtsev, A.G. & Podjarny, A.D. On the ab Initio solution of the phase problem for macromolecules at very low resolution. II. Generalized likelihood based approach to cluster discrimination. Acta Crystallogr. D 54, 726-734 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 726-734
    • Lunin, V.Y.1    Lunina, N.L.2    Petrova, T.E.3    Urzhumtsev, A.G.4    Podjarny, A.D.5
  • 14
    • 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, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 16
    • 0030933355 scopus 로고    scopus 로고
    • Template convolution to enhance or detect structural features in macromolecular electron-density maps
    • Kleywegt, G.J. & Jones, T.A. Template convolution to enhance or detect structural features in macromolecular electron-density maps. Acta Crystatlogr. D 53, 179-185 (1997).
    • (1997) Acta Crystatlogr. D , vol.53 , pp. 179-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 17
    • 0032529002 scopus 로고    scopus 로고
    • The crystal structure of Leishmania major surface proteinase leishmanolysin (gp63)
    • Schlagenhauf, E., Etges, R. & Metcalf, P. The crystal structure of Leishmania major surface proteinase leishmanolysin (gp63). Structure 6, 1035-1046 (1998).
    • (1998) Structure , vol.6 , pp. 1035-1046
    • Schlagenhauf, E.1    Etges, R.2    Metcalf, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.