Single-Particle Cryo-EM at Crystallographic Resolution

被引：400

作者：

Cheng, Yifan ^{[1
]}

机构：

[1] Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94158 USA

来源：

CELL | 2015年 / 161卷 / 03期

关键词：

MAXIMUM-LIKELIHOOD METHODS; X-RAY CRYSTALLOGRAPHY; BEAM-INDUCED MOTION; ELECTRON CRYOMICROSCOPY; CRYOELECTRON MICROSCOPY; ATOMIC-RESOLUTION; MOLECULAR ARCHITECTURE; PROTEIN CRYSTALS; RADIATION-DAMAGE; 26S PROTEASOME;

D O I：

10.1016/j.cell.2015.03.049

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Until only a few years ago, single-particle electron cryo-microscopy (cryo-EM) was usually not the first choice for many structural biologists due to its limited resolution in the range of nanometer to subnanometer. Now, this method rivals X-ray crystallography in terms of resolution and can be used to determine atomic structures of macromolecules that are either refractory to crystallization or difficult to crystallize in specific functional states. In this review, I discuss the recent breakthroughs in both hardware and software that transformed cryo-microscopy, enabling understanding of complex biomolecules and their functions at atomic level.

引用

页码：450 / 457

页数：8

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