ULTRA HIGH RESOLUTION STRUCTURE OF NG GTPASE

NG GTPase 的超高分辨率结构

• 批准号: 6119492
• 负责人: DOUGLAS M FREYMANN
• 金额: --
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-03-01 至 2000-04-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6119492
• 关键词: biomaterials; proteins

The NG GTPase domain of Ffh, the bacterial homolog of the signal sequence recognition protein SRP54, reveals several unique features that should contribute to our understanding of GTPase structure-function in general. Crystals of the apo-form of the domain diffract to beyond 1.0 E resolution at a synchrotron X-ray source (SSRL BL 7-1), and crystals of the GDP-bound domain diffract almost as well. During previous work we have developed methods for efficient data collection from these crystals to that resolution. Our efforts are now directed at obtaining complete well measured data to ultra-high resolution from both crystal forms.

Ffh的NG GT3结构域，信号的细菌同源物 序列识别蛋白SRP 54，揭示了几个独特的功能 这应该有助于我们理解GTMEN 一般的结构功能。 晶体的apo形式的域 在同步加速器X射线源上获得超过1.0E的分辨率 (SSRL BL 7-1），GDP结合域的晶体几乎充当 好. 在以前的工作中，我们已经开发了有效的方法， 从这些晶体收集数据到那个分辨率。 我们的努力 现在致力于获得完整的井测数据， 两种晶体形式的超高分辨率。