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Curr Opin Struct Biol. 2016 Dec;41:194-202. doi: 10.1016/j.sbi.2016.07.009. Epub 2016 Aug 20.

Resolution advances in cryo-EM enable application to drug discovery.

Author information

1
Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: ss1@nih.gov.
2
Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
3
University of Virginia, Charlottesville, VA 22908, USA.

Abstract

The prospect that the structures of protein assemblies, small and large, can be determined using cryo-electron microscopy (cryo-EM) is beginning to transform the landscape of structural biology and cell biology. Great progress is being made in determining 3D structures of biological assemblies ranging from icosahedral viruses and helical arrays to small membrane proteins and protein complexes. Here, we review recent advances in this field, focusing especially on the emerging use of cryo-EM in mapping the binding of drugs and inhibitors to protein targets, an application that requires structure determination at the highest possible resolutions. We discuss methods used to evaluate the information contained in cryo-EM density maps and consider strengths and weaknesses of approaches currently used to measure map resolution.

PMID:
27552081
PMCID:
PMC5154827
DOI:
10.1016/j.sbi.2016.07.009
[Indexed for MEDLINE]
Free PMC Article

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