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      How cryo-EM is revolutionizing structural biology.

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          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.

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          Author and article information

          Journal
          Trends Biochem. Sci.
          Trends in biochemical sciences
          0968-0004
          0968-0004
          Jan 2015
          : 40
          : 1
          Affiliations
          [1 ] MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, CB2 0QH, UK.
          [2 ] MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, CB2 0QH, UK. Electronic address: scheres@mrc-lmb.cam.ac.uk.
          Article
          S0968-0004(14)00187-X
          10.1016/j.tibs.2014.10.005
          25544475
          d78b09d4-45bd-4cab-85d3-2740d8fb09bf
          Copyright © 2014 Elsevier Ltd. All rights reserved.
          History

          3D reconstruction,cryo-electron microscopy,electron detection,image processing,macromolecular complexes,maximum-likelihood optimization,single-particle analysis

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