CRYSTAL STRUCTURE OF MOLECULAR CHAPERONE

分子伴侣的晶体结构

• 批准号: 6586751
• 负责人: LARRY E VICKERY
• 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/6586751
• 关键词: bioimaging /biomedical imaging; biomaterials; biomedical resource; proteins; radiography; structural biology

Molecular chaperones play key roles in protein folding, transport across membranes, and in response to stressful stimuli. We have recently succeeded in overexpressing, purifying and crystallizing Hsc20, a J-motif co-chaperone protein which regulates the chaperone Hsc66 in E. coli. A native data set to 1.9 E resolution has been collected, and heavy atom derivatives are now being characterized in order to solve the structure by multiple isomorphous replacement methods.

分子伴侣在蛋白质折叠，传输中起关键作用 跨膜，并响应压力刺激。 我们有 最近成功过表达，净化和结晶 HSC20，一种调节伴侣的J-MOTIF副酮蛋白 大肠杆菌中的HSC66。 本机数据集达到1.9 e分辨率已有 收集的，重的原子衍生物现在被表征 为了通过多种同构替换来解决结构 方法。