Observation of unstable species in enzyme-catalyzed transformations using protein crystallography

被引：40

作者：

Petsko, GA

Ringe, D

机构：

[1] Brandeis Univ, Dept Biochem, Waltham, MA 02454 USA

[2] Brandeis Univ, Dept Chem, Waltham, MA 02454 USA

[3] Brandeis Univ, Rosenstiel Basic Med Sci Res Ctr, Waltham, MA 02454 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2000年 / 4卷 / 01期

关键词：

D O I：

10.1016/S1367-5931(99)00057-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recent advances in rapid X-ray diffraction data collection methods, cryocrystallography, and other techniques have made it possible to visualize short-lived species in enzyme-catalyzed reactions directly at atomic resolution for a significant number of crystalline enzymes. The Wide range of reaction types, intermediate lifetimes, and crystal characteristics means that different methods must be employed in each case, but there are enough examples now of successful structure determinations of normally unstable species to suggest guidelines for future investigations.

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页码：89 / 94

页数：6

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