Format

Send to

Choose Destination
Trends Biochem Sci. 2015 Jan;40(1):49-57. doi: 10.1016/j.tibs.2014.10.005. Epub 2014 Nov 7.

How cryo-EM is revolutionizing structural biology.

Author information

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.

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.

KEYWORDS:

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

PMID:
25544475
DOI:
10.1016/j.tibs.2014.10.005
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center