Macromolecular Crystallography Research with Synchrotron Radiation

利用硫原子提供的非常小的异常衍射信号， 固有地存在于所有蛋白质中的半胱氨酸和甲硫氨酸残基可以成功地 用来解析蛋白质的晶体结构这种方法，部分由我们开创， 目前越来越受欢迎，并可能成为实践中的常规技术， 大分子晶体学衍射数据达到0.65的极高分辨率 埃测量使用同步辐射，和完善的模型揭示了 溶菌酶分子前所未有的结构细节。观察到的非常细微的特征 在这种结构中，将有助于改善用于常规的立体化学库。 在较低的分辨率下细化蛋白质晶体结构。我们参加了几个 各种生物重要蛋白质的合作结构项目，如 对线粒体mRNA降解体中的细菌和人类酶活性的研究。

Utilization of a very small anomalous diffraction signal provided by sulfur atoms of the cysteine and methionine residues, intrinsically present in all proteins can be succssfully used to solve crystal structures of proteins. This approach, in part pioneered by us, is currently gaining increasoing popularity and may become a routine technique in the practice of macromolecular crystallography. The diffraction data to extremely high resolution of 0.65 angstrom were measured using synchrotron radiation, and the refined model reveals the unprecedented structgural details of the molecule of lysozyme. The observed very fine features in this structure will serve to improve the stereochemical libraries used for routine refinement of protein crystal structures at lower resolution. We participated in several collaborative structural projects on various biologically important proteins, such as the studies of the bacterial and human enzymes active in the mitochondrial mRNA degradosome.