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Volumn 22, Issue 13, 2006, Pages 1660-1661

Map2mod - A server for evaluation of crystallographic models and their agreement with electron density maps

Author keywords

[No Author keywords available]

Indexed keywords

WATER;

EID: 33745608216     PISSN: 13674803     EISSN: 13674811     Source Type: Journal    
DOI: 10.1093/bioinformatics/btl152     Document Type: Article
Times cited : (4)

References (13)
  • 1
    • 0033954256 scopus 로고    scopus 로고
    • The protein Data Bank
    • Berman, H.M. et al, (2000) The protein Data Bank. Nucleic Acids Res., 28, 235-242.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 235-242
    • Berman, H.M.1
  • 2
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, number 4
    • Collaborative Computational Project, number 4. (1994), The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr., 50, 760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 3
  • 4
    • 0344186399 scopus 로고    scopus 로고
    • Errors in protein structures
    • Hook, R.W. et al. (1996) Errors in protein structures. Nature, 381, 272.
    • (1996) Nature , vol.381 , pp. 272
    • Hook, R.W.1
  • 6
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A. et al. (1993) PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1
  • 7
    • 0037441653 scopus 로고    scopus 로고
    • Structure validation by Calpha geometry: Phi,psi, and Cbeta deviation
    • Lovell, S.C. et al. (2003) Structure validation by Calpha geometry: phi,psi, and Cbeta deviation. Proteins, 50, 437-450, http:// kinemage.biochem.duke.edu/molprobity/main.php.
    • (2003) Proteins , vol.50 , pp. 437-450
    • Lovell, S.C.1
  • 8
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee, D.E. (1999) XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol., 125, 156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 9
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of Macromolecular structures by Maximum likelihood method
    • Murshudov, G.N. et al. (1997) Refinement of Macromolecular structures by Maximum likelihood method. Acta Crystallogr. D Biol. Crystallogr., 53, 240-255.
    • (1997) Acta Crystallogr. D Biol. Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1
  • 10
    • 0347364621 scopus 로고    scopus 로고
    • Protein flexibility and intrinsic disorder
    • Radivojac, P. et al. (2004) Protein flexibility and intrinsic disorder. Protein Sci., 13, 71-80.
    • (2004) Protein Sci. , vol.13 , pp. 71-80
    • Radivojac, P.1
  • 12
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedure for evaluating the quality of macromolecular stracture-factor data and their agreement with atomic model
    • Vaguine, A.A. et al. (1999) SFCHECK: A unified set of procedure for evaluating the quality of macromolecular stracture-factor data and their agreement with atomic model. Acta Crystallogr. D Biol. Crystallogr., 55, 191-205.
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 191-205
    • Vaguine, A.A.1
  • 13
    • 16644393507 scopus 로고    scopus 로고
    • Automated and accurate deposition of structures solved by X-ray diffraction to the Protein Data Bank
    • Yang, H. et al. (2004) Automated and accurate deposition of structures solved by X-ray diffraction to the Protein Data Bank. Acta Crystallogr. D Biol. Crystallogr., 60, 1833-1839.
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 1833-1839
    • Yang, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.