Protein structure determination by electron cryo-microscopy
Protein structure determination by electron cryo-microscopy
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DOI：
10.1016/j.coph.2009.04.006
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发表时间：
2009-10-01
影响因子：
4
通讯作者：
Venien-Bryan, Catherine
中科院分区：
文献类型：
--
作者：
Jonic, Slavica;Venien-Bryan, Catherine
透射式电子冷冻显微镜(CryoEM)是蛋白质和生物大分子组装体结构分析的通用工具。在这篇综述中，我们简要介绍了在低温电子显微镜中使用的方法及其最新进展。这些最新进展为大分子络合物的三维结构测定提供了令人兴奋的机会，这些络合物要么太大，要么太多，无法用传统的X射线结晶学或核磁共振(核磁共振)进行研究。结合电子显微镜和X射线结晶学的数据，通常有助于理解蛋白质或大分子复合体的功能。因此，我们将简要概述合并来自不同技术的数据以解释EM结构所涉及的计算技术。
Transmission electron cryo-microscopy (cryoEM) is a versatile tool in the structural analysis of proteins and biological macromolecular assemblies. In this review, we present a brief survey of the methods used in cryoEM, and their current developments. These latest advances provide exciting opportunities for the three-dimensional structural determination of macromolecular complexes that are either too large or too heterogeneous to be investigated by conventional X-ray crystallography or nuclear magnetic resonance (NMR). The endeavour of understanding the function of protein or macromolecular complex is often helped by combining data from electron microscopy and X-ray crystallography. We will thus provide a brief overview of the computational techniques involved in combining data from different techniques for the interpretation of the EM structure.