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Curr Opin Struct Biol. 2019 Jul 27;58:166-174. doi: 10.1016/j.sbi.2019.06.009. [Epub ahead of print]

Interpretation of medium resolution cryoEM maps of multi-protein complexes.

Author information

1
MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom. Electronic address: acasanal@mrc-lmb.cam.ac.uk.
2
MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.
3
MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom. Electronic address: passmore@mrc-lmb.cam.ac.uk.

Abstract

Electron cryo-microscopy (cryoEM) is used to determine structures of biological molecules, including multi-protein complexes. Maps at better than 3.0Å resolution are relatively straightforward to interpret since atomic models of proteins and nucleic acids can be built directly. Still, these resolutions are often difficult to achieve, and map quality frequently varies within a structure. This results in data that are challenging to interpret, especially when crystal structures or suitable homology models are not available. Recent advances in mass spectrometry techniques, computational methods and model building tools facilitate subunit/domain fitting into maps, elucidation of protein contacts, and de novo generation of atomic models. Here, we review techniques for map interpretation and provide examples from recent studies of multi-protein complexes.

PMID:
31362190
DOI:
10.1016/j.sbi.2019.06.009

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