Macromolecular Crystallography Research with Synchrotron Radiation

同步辐射高分子晶体学研究

• 批准号: 8157288
• 负责人: ZBIGNIEW DAUTER
• 金额: $ 140.44万
• 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/8157288
• 关键词: Crystallography; Research; synchrotron radiation

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.

利用由半胱氨酸和甲硫氨酸残基的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，可以成功地用于解析蛋白质的晶体结构。这种方法，部分是由我们开创的，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。使用同步辐射测量了0.65埃的极高分辨率的衍射数据，改进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。在该结构中观察到的非常精细的特征将用于改进用于在较低分辨率下常规细化蛋白质晶体结构的立体化学库。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，例如冷适应酯酶和DNA结合蛋白Taz2的研究。