Macromolecular Crystallography Research with Synchrotron

最近，我们已经证明，所有蛋白质中固有存在的硫原子的非常小的异常衍射信号(不到总信号的0.5%)可以成功地用于解析蛋白质的晶体结构。该方法有可能成为大分子结晶学实践中的常规技术。用同步辐射测量了0.65埃的极高分辨率的衍射数据，改进后的模型揭示了溶菌酶分子前所未有的结构细节。对水产水母单链DNA结合蛋白的结构进行了解析，结果表明该蛋白的2-OB结构域亚单位形成的寡聚体类似于其他细菌中更典型的单结构域SSB。解决了致尿性大肠杆菌侵袭DRAD的晶体结构，揭示了细菌在形成侵袭性纤维时所利用的异常的自我互补的聚集机制。我们参与了几个关于各种生物重要蛋白质的合作结构项目，例如神经性同源两个结构域或ArgAerte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.