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CryoEM structure refinement by integrating NMR chemical shifts with molecular dynamics simulations

Abstract:

Single particle cryoEM has emerged as a powerful method for structure determination of proteins and complexes, complementing X-ray crystallography and NMR spectroscopy. Yet, for many systems, the resolution of cryoEM density map has been limited to 4-6 Å, which only allows for resolving bulky amino acids side chains, thus hindering accurate model building from the density map. On the other hand, experimental chemical shifts (CS) from solution and solid state MAS NMR spectra provide atomic lev...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Accepted manuscript

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Files:
Publisher copy:
10.1021/acs.jpcb.6b13105

Authors


Perilla, JR More by this author
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Grant:
P50 GM082251, P41 GM104601, R01 GM067887, P30GM103519; P30GM110758
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Grant:
CHE0959496; OCI-0725070; ACI-1238993
Publisher:
American Chemical Society Publisher's website
Journal:
Journal of Physical Chemistry B Journal website
Volume:
121
Issue:
15
Pages:
3853–3863
Publication date:
2017-02-09
Acceptance date:
2017-02-09
DOI:
EISSN:
1520-5207
ISSN:
1520-6106
Pubs id:
pubs:681925
URN:
uri:21617d98-f1be-4909-811a-ab6f2cd9ac65
UUID:
uuid:21617d98-f1be-4909-811a-ab6f2cd9ac65
Local pid:
pubs:681925
Language:
English
Keywords:

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