CRYOPRESERVED CRYSTALS OF HEMOLIN, FASCICLIN III & HIGH PH NEONATAL FC RECEPTOR

冷冻保存的血红素晶体，FASCICLIN III

• 批准号: 6586735
• 负责人: Pamela J Bjorkman
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-03-01 至 2003-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6586735
• 关键词: bioimaging /biomedical imaging; biomaterials; biomedical resource; proteins; radiography; structural biology

Proper function of a-lytic protease requires the presence of its N-terminal pro region, which catalyzes an as yet unidentified step in the folding of this enzyme. In order to better understand the folding mechanism, we are using x-ray crystallography to determine the structure of the pro region, both by itself and in a complex with folded protease. We have engineered several mutants containing cysteines to facilitate the preparation of heavy atom derivatives for multiple isomorphous replacement.

α-裂解蛋白酶的正常功能需要其 N-末端pro区，其催化一个尚未鉴定的步骤， 这种酶的折叠。 为了更好地理解折叠 机制，我们正在使用X射线晶体学来确定 亲区域的结构，无论是本身还是与 折叠蛋白酶 我们设计了几种突变体 半胱氨酸，以便于制备用于 多次同晶置换