MULTIWAVELENGTH ANOMALOUS DISPERSION DATA COLLECTION FROM E COLI FABH CRYSTALS

从大肠杆菌 FABH 晶体中收集多波长反常色散数据

• 批准号: 6220525
• 负责人: STEPHEN W WHITE
• 金额: $ 1.36万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-08-15 至 2000-08-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6220525
• 关键词: bioimaging /biomedical imaging; biological products; biomedical resource; proteins; radiography; structural biology

We propose to determine the structure of a complex between the E. coli chaperonin GroEL (Cpn60) and the gp 5 capsid protein of bacteriophage HK97. Suitable crystals have been obtained, they can be flash frozen at -160oC and preliminary data have been collected at CHESS to 3.6
resolution. Chaperonins, including members of the Cpn60 family are a ubiuitous class of proteins that assist in protein folding in vivo by binding to partially folded proteins; this prevents aggregation and may unfold off pathway intermediates and direct them back into the correct folding pathway. The gp 5 protein is a natural substrate of GroEL; it is the major capsid protein in the ocosahedral head of the lambdoid bacteriophage HK97. The unit cell parameters are: a = 138.0,b = 270.9, c = 155.4
, b = 101.4o. The Space Group is P2. The asymmetric unit contains one 14mer of GroEL and one subunit of the HK97 gp5 protein, i.e. it is the smallest asymmetric unti that could contain a complete complex of this type.

我们建议确定E.之间的复合物的结构。 大肠杆菌伴侣颗粒（CPN60）和GP 5帽蛋白 噬菌体HK97。 已经获得了合适的晶体，它们可以是 在-160oc中冷冻的闪光和初步数据已收集 国际象棋至3.6分辨率。 伴侣，包括 CPN60家族是一类蛋白质类别，可帮助蛋白质 通过与部分折叠的蛋白结合在体内折叠；这可以防止 聚集并可能从中间路径中展开并指导它们 回到正确的折叠路径。 GP 5蛋白是自然的 凹槽的底物；它是甲状腺体的主要衣壳蛋白 lambdoid噬菌体HK97的头。 单元电池参数 为：a = 138.0，b = 270.9，c = 155.4，b = 101.4o。 空间群体 是P2。 不对称单元包含一个14mer的凹槽和一个 HK97 GP5蛋白的亚基，即它是最小的不对称 可以包含这种类型的完整复合物的UNTI。