Petsko G A, Ringe D
Departments of Biochemistry and Chemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454-9110, USA.
Curr Opin Chem Biol. 2000 Feb;4(1):89-94. doi: 10.1016/s1367-5931(99)00057-5.
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.
快速X射线衍射数据收集方法、低温晶体学及其他技术的最新进展，使得在原子分辨率下直接观察大量结晶酶催化反应中的短寿命物种成为可能。反应类型、中间体寿命和晶体特性的广泛差异意味着每种情况都必须采用不同的方法，但目前已有足够多成功测定通常不稳定物种结构的例子，可为未来的研究提供指导方针。
