How cryo-EM is revolutionizing structural biology

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


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.

Publication types

  • Review

MeSH terms

  • Cryoelectron Microscopy*
  • Crystallography, X-Ray
  • Image Processing, Computer-Assisted*
  • Imaging, Three-Dimensional / methods*
  • Macromolecular Substances / chemistry*
  • Molecular Biology / methods
  • Protein Conformation


  • Macromolecular Substances