Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 294, Issue 13, Pages 5181-5197Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.REV118.005602
Keywords
protein structure; cryo-electron microscopy; single-particle analysis; protein-protein interaction; structural biology; atomic resolution
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Funding
- National Institutes of Health [DP5 OD021396, R01 AI136680, U54 GM103368]
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Cryogenic electron microscopy (cryo-EM) enables structure determination of macromolecular objects and their assemblies. Although the techniques have been developing for nearly four decades, they have gained widespread attention in recent years due to technical advances on numerous fronts, enabling traditional microscopists to break into the world of molecular structural biology. Many samples can now be routinely analyzed at near-atomic resolution using standard imaging and image analysis techniques. However, numerous challenges to conventional workflows remain, and continued technical advances open entirely novel opportunities for discovery and exploration. Here, I will review some of the main methods surrounding cryo-EM with an emphasis specifically on single-particle analysis, and I will highlight challenges, open questions, and opportunities for methodology development.
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