Macromolecular Crystallography Research with Synchrotron

最近，我们已经证明，一个非常小的异常衍射信号（小于总数的0.5%）的硫原子，本质上存在于所有蛋白质可以成功地用于解决蛋白质的晶体结构。这种方法可能成为大分子晶体学实践中的一种常规技术。利用同步辐射测量了极高分辨率0.65埃的衍射数据，改进后的模型揭示了溶菌酶分子前所未有的结构细节。该单链dna结合蛋白的结构得到了解决，表明该蛋白的两个ob结构域亚基形成了类似于其他细菌的更典型的单结构域ssb的低聚物。对尿路致病性大肠杆菌侵入蛋白DraD的晶体结构进行了解析，揭示了其独特的自互补聚集机制，并利用其形成侵入性原纤维。我们参与了多个合作结构项目，研究各种重要的生物学蛋白，如神经同源二结构域或argonaute蛋白。

Recently we have shown that a very small anomalous diffraction signal (less than 0.5% of the total) of sulfur atoms, intrinsically present in all proteins can be succssfully used to solve crystal structures of proteins. This approach may become a routine technique in the practice olf 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 structure of the single-stranded DNA-binding protein from T. aquaticus was solved showing that the two-OB domain subunit of this protein forms oligomers analogous to the more typical, single-domain SSBs from other bacteria. The crystal structure of the uropathogenic E. coli invasin DraD was solved and revealed the unusual self-complementing mwechanism of aggregation, utilized by the becteria in formation of invasive fibrils. We participated in several collaborative structural projects on various biologically important proteins, such as Nervy homology two domain or the argonaute protein.