Extending X-ray Crystallography to Allow Structure Retrieval from Highly Disordered Crystals and Nanocrystals

扩展 X 射线晶体学以实现高度无序晶体和纳米晶体的结构检索

• 批准号: FT130101797
• 负责人: Prof Brian Abbey
• 金额: $ 45.08万
• 依托单位: La Trobe University
• 依托单位国家: 澳大利亚
• 项目类别: ARC Future Fellowships
• 财政年份: 2014
• 资助国家: 澳大利亚
• 起止时间: 2014-02-24 至 2018-11-30
• 项目状态: 已结题
• 来源: https://dataportal.arc.gov.au/RGS/Web/Grants/FT130101797
• 关键词: Extending; ray; Crystallography; Allow; Structure

X-ray crystallography is one of the most important tools in structural biology, responsible for over 80 per cent of the protein structures solved today. Obtaining X-ray diffraction data however is critically dependent on having large, high quality crystals. Many proteins, particularly membrane proteins, only form nanocrystals or crystals of poor quality which prevents their structure being solved. This project aims to combine ideas from X-ray coherent diffraction imaging and X-ray crystallography to develop a method that can be used for structure retrieval from nanocrystals or crystals which are highly disordered. A particular emphasis will be placed on solving the structure of membrane proteins which are of special importance in drug development.

X 射线晶体学是结构生物学中最重要的工具之一，目前解决的蛋白质结构中 80% 以上都是由 X 射线晶体学完成的。然而，获得 X 射线衍射数据关键取决于是否拥有大型、高质量的晶体。许多蛋白质，特别是膜蛋白，只能形成纳米晶体或质量较差的晶体，这阻碍了其结构的解析。该项目旨在结合 X 射线相干衍射成像和 X 射线晶体学的思想，开发一种可用于从高度无序的纳米晶体或晶体中进行结构检索的方法。将特别强调解决膜蛋白的结构，这在药物开发中特别重要。