Observation of unstable species in enzyme-catalyzed transformations using protein crystallography.
Observation of unstable species in enzyme-catalyzed transformations using protein crystallography.
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DOI：
10.1016/s1367-5931(99)00057-5
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发表时间：
2000-02
影响因子：
7.8
通讯作者：
G. Petsko;D. Ringe
中科院分区：
文献类型：
--
作者：
G. Petsko;D. Ringe
在快速X射线衍射数据收集方法、结晶学和其他技术方面的最新进展使直接以原子分辨率显示大量结晶酶的酶催化反应中的短暂物种成为可能。反应类型、中间寿命和晶体特性的广泛范围意味着必须在每种情况下采用不同的方法，但现在有足够多的成功测定通常不稳定物种的结构的例子，为未来的研究提供指导方针。
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.