How cryo-EM is revolutionizing structural biology. Issue 1 (January 2015)

• Record Type: Journal Article
• Authors: Bai, Xiao-chen; McMullan, Greg; Scheres, Sjors H.W
• Is Part Of: Trends in biochemical sciences. Volume 40:Issue 1(2015)
• Page Start: 49
• Page End: 57
• Publication Date: 2015-01
• Subjects: macromolecular complexes -- single-particle analysis -- cryo-electron microscopy -- image processing -- 3D reconstruction -- electron detection -- maximum-likelihood optimization; Biochemistry -- Periodicals; 572
• DOI: 10.1016/j.tibs.2014.10.005
• Languages: English
• ISSNs: 0968-0004

Abstract

Highlights: Cryo-EM single-particle analysis reaches near-atomic resolution for a wide variety of specimens. Direct electron detectors yield images of unprecedented quality. New movie-processing methods correct for beam-induced sample movements. New classification methods separate images of different structures. Abstract : 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.