Macromolecular Crystallography Research with Synchrotron Radiation

利用半胱氨酸和蛋氨酸残基的硫原子提供的非常小的异常衍射信号，本质上存在于所有蛋白质中，可以成功地用于解决蛋白质的晶体结构。这种方法在一定程度上是由我们首创的，目前越来越受欢迎，并可能成为大分子晶体学实践中的常规技术。利用同步辐射测量了极高分辨率为0.65埃的衍射数据，改进后的模型揭示了所研究分子前所未有的结构细节。包括成键电子。在这种结构中观察到的非常精细的特征将有助于改进用于低分辨率蛋白质晶体结构常规细化的立体化学文库。我们参与了多个具有重要生物学意义的蛋白质的合作结构项目，如冷适应酯酶和dna结合蛋白Taz2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 structural details of the investigated molecules. including bonding electrons. The observed very fine fatures 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 cold-adapted esterase and DNA-binding protein Taz2.