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Volumn 57, Issue 4, 2004, Pages 869-873

Crystal structure of hypothetical protein PH0642 from Pyrococcus horikoshii at 1.6Å resolution

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; HYPOTHETICAL PROTEIN; PROTEIN PH0642; UNCLASSIFIED DRUG;

EID: 10344224511     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20259     Document Type: Article
Times cited : (37)

References (17)
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    • De La Fortelle, E.1    Bricogne, G.2
  • 6
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    • Terwilliger TC. Maximum-likelihood density modification. Acta Crystallogr D 2000;56:965-972.
    • (2000) Acta Crystallogr D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
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    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
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    • Protein structure comparison by alignment of distance matrices
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  • 14
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    • Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft
    • Wang WC, Hsu WH, Chien FT, Chen CY. Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft. J Mol Biol 2001;306:251-261.
    • (2001) J Mol Biol , vol.306 , pp. 251-261
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  • 15
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    • Detection of covalent enzymesubstrate complexes of nitrilase by ion-spray mass spectroscopy
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.