Macromolecular Crystallography Research with Synchrotron

同步加速器高分子晶体学研究

• 批准号: 7338501
• 负责人: ZBIGNIEW DAUTER
• 金额: --
• 依托单位: DIVISION OF BASIC SCIENCES - NCI
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/7338501
• 关键词: Macromolecular; Crystallography; Research; Synchrotron

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.

最近，我们已经表明，一个非常小的异常衍射信号（小于总数的0.5%）的硫原子，固有地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常规技术。用同步辐射测量了衍射数据，达到了0.65埃的极高分辨率，精细模型揭示了溶菌酶分子前所未有的结构细节。对T. aquaticus的结果表明，该蛋白质的两个OB结构域亚基形成类似于来自其他细菌的更典型的单结构域SSB的寡聚体。尿致病性E. coli invasin DraD的表达，揭示了该菌在形成侵袭原纤维时所利用的不寻常的自互补聚集机制。我们参与了几个关于各种生物学重要蛋白质的合作结构项目，例如Nervy同源性两个结构域或argonaute蛋白。