How cryo-EM is revolutionizing structural biology

被引:730
作者
Bai, Xiao-Chen [1 ]
McMullan, Greg [1 ]
Scheres, Sjors H. W. [1 ]
机构
[1] MRC, Mol Biol Lab, Cambridge CB2 0QH, England
基金
英国医学研究理事会;
关键词
macromolecular complexes; single-particle analysis; cryo-electron microscopy; image processing; 3D reconstruction; electron detection; maximum-likelihood optimization; TRANSMISSION ELECTRON-MICROSCOPY; SINGLE-PARTICLE RECONSTRUCTION; LARGE RIBOSOMAL-SUBUNIT; ACTIVE PIXEL SENSOR; ATOMIC-RESOLUTION; 3-DIMENSIONAL RECONSTRUCTION; CRYOELECTRON MICROSCOPY; ANGSTROM RESOLUTION; ESCHERICHIA-COLI; PROTEIN CRYSTALS;
D O I
10.1016/j.tibs.2014.10.005
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
For many years, structure determination of biological macromolecules by cryo-electron microscopy (cryo-EM) was limited to large complexes or low-resolution models. With recent advances in electron detection and image processing, the resolution by cryo-EM is now beginning to rival X-ray crystallography. A new generation of electron detectors record images with unprecedented quality, while new image-processing tools correct for sample movements and classify images according to different structural states. Combined, these advances yield density maps with sufficient detail to deduce the atomic structure for a range of specimens. Here, we review the recent advances and illustrate the exciting new opportunities that they offer to structural biology research.
引用
收藏
页码:49 / 57
页数:9
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