Fujiyoshi Yoshinori
Cellular and Structural Physiology Institute, Nagoya University, Graduate School of Pharmaceutical Sciences, Nagoya University.
Proc Jpn Acad Ser B Phys Biol Sci. 2015;91(9):447-68. doi: 10.2183/pjab.91.447.
Electron crystallography is especially useful for studying the structure and function of membrane proteins - key molecules with important functions in neural and other cells. Electron crystallography is now an established technique for analyzing the structures of membrane proteins in lipid bilayers that closely simulate their natural biological environment. Utilizing cryo-electron microscopes with helium-cooled specimen stages that were developed through a personal motivation to understand the functions of neural systems from a structural point of view, the structures of membrane proteins can be analyzed at a higher than 3 Å resolution. This review covers four objectives. First, I introduce the new research field of structural physiology. Second, I recount some of the struggles involved in developing cryo-electron microscopes. Third, I review the structural and functional analyses of membrane proteins mainly by electron crystallography using cryo-electron microscopes. Finally, I discuss multifunctional channels named "adhennels" based on structures analyzed using electron and X-ray crystallography.
电子晶体学对于研究膜蛋白的结构和功能特别有用——膜蛋白是在神经细胞和其他细胞中具有重要功能的关键分子。电子晶体学现在是一种成熟的技术，用于分析脂质双分子层中膜蛋白的结构，这种脂质双分子层能紧密模拟其天然生物环境。利用通过个人从结构角度理解神经系统功能的动机而开发的带有氦冷却样品台的低温电子显微镜，可以以高于3埃的分辨率分析膜蛋白的结构。本综述涵盖四个目标。第一，我介绍结构生理学这一新的研究领域。第二，我讲述在开发低温电子显微镜过程中所经历的一些困难。第三，我主要回顾使用低温电子显微镜通过电子晶体学对膜蛋白进行的结构和功能分析。最后，我基于使用电子晶体学和X射线晶体学分析的结构，讨论名为“粘附通道”的多功能通道。
