Walz T, Grigorieff N
Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, United Kingdom
J Struct Biol. 1998;121(2):142-61. doi: 10.1006/jsbi.1998.3945.
Electron microscopy has become a powerful technique, along with X-ray crystallography and nuclear magnetic resonance spectroscopy, to study the three-dimensional structure of biological molecules. It has evolved into a number of methods dealing with a wide range of biological samples, with electron crystallography of two-dimensional crystals being so far the only method allowing data collection at near-atomic resolution. In this paper, we review the methodology of electron crystallography and its application to membrane proteins, starting with the pioneering work on bacteriorhodopsin, which led to the first visualization of the secondary structure of a membrane protein in 1975. Since then, improvements in instrumentation, sample preparation, and data analysis have led to atomic models for bacteriorhodopsin and light-harvesting complex II from higher plants. The structures of many more membrane proteins have been studied by electron crystallography and in this review examples are included where a resolution of better than 10 Å has been achieved. Indeed, in some of the given examples an atomic model can be expected in the near future. Finally, a brief outlook is given on current and future developments of electron crystallographic methods. Copyright 1998 Academic Press.
电子显微镜已成为一种强大的技术，与X射线晶体学和核磁共振光谱学一起，用于研究生物分子的三维结构。它已发展出多种处理广泛生物样品的方法，二维晶体的电子晶体学是迄今为止唯一能够在近原子分辨率下收集数据的方法。在本文中，我们回顾电子晶体学的方法及其在膜蛋白中的应用，从细菌视紫红质的开创性工作开始，该工作在1975年首次实现了膜蛋白二级结构的可视化。从那时起，仪器设备、样品制备和数据分析方面的改进已导致获得了细菌视紫红质和高等植物光捕获复合物II的原子模型。更多膜蛋白的结构已通过电子晶体学进行了研究，在本综述中包含了一些分辨率优于10 Å的实例。实际上，在一些给定的实例中，预计在不久的将来可以得到原子模型。最后，对电子晶体学方法的当前和未来发展作了简要展望。版权所有1998年学术出版社。
