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Annu Rev Biomed Eng. 2019 Jun 4;21:395-415. doi: 10.1146/annurev-bioeng-060418-052453. Epub 2019 Mar 20.

Frontiers in Cryo Electron Microscopy of Complex Macromolecular Assemblies.

Author information

1
Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, Bethesda, Maryland 20814, USA; email: jana.ognjenovic@nih.gov , reinhard.grisshammer2@nih.gov.
2
University of British Columbia, Vancouver, British Columbia V6T 1Z2, Canada; email: Sriram.Subramaniam@ubc.ca.

Abstract

In recent years, cryo electron microscopy (cryo-EM) technology has been transformed with the development of better instrumentation, direct electron detectors, improved methods for specimen preparation, and improved software for data analysis. Analyses using single-particle cryo-EM methods have enabled determination of structures of proteins with sizes smaller than 100 kDa and resolutions of ∼2 Å in some cases. The use of electron tomography combined with subvolume averaging is beginning to allow the visualization of macromolecular complexes in their native environment in unprecedented detail. As a result of these advances, solutions to many intractable challenges in structural and cell biology, such as analysis of highly dynamic soluble and membrane-embedded protein complexes or partially ordered protein aggregates, are now within reach. Recent reports of structural studies of G protein-coupled receptors, spliceosomes, and fibrillar specimens illustrate the progress that has been made using cryo-EM methods, and are the main focus of this review.

KEYWORDS:

G protein–coupled receptor; cryo electron tomography; cryo-EM; fibril; single-particle analysis; spliceosome

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