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Volumn 3, Issue 10, 1995, Pages 991-996

Direct measurement of reactivity in the protein crystal by steady-state kinetic studies

Author keywords

[No Author keywords available]

Indexed keywords

CHYMOTRYPSIN; ISOCITRATE DEHYDROGENASE; PROTEIN;

EID: 0029645585     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(01)00235-0     Document Type: Article
Times cited : (25)

References (23)
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    • Millisecond X-ray diffraction and the first electron density map from Laue photographs of a protein crystal
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  • 19
    • 0025275582 scopus 로고
    • Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis
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    • (1990) Nature , vol.345 , pp. 309-315
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  • 21
    • 0027411179 scopus 로고
    • The hydrolytic water molecule in trypsin, revealed by time-resolved Laue crystallography
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    • (1993) Science , vol.259 , pp. 669-673
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  • 22
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    • Laue diffraction study on the structure of cytochrome c peroxidase compound
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    • (1994) Structure , vol.2 , pp. 201-208
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    • Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase
    • 95282016
    • (1995) Science , vol.268 , pp. 1312-1318
    • Bolduc1    Stoddard2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.