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Combined 1H-detected solid-state NMR spectroscopy and electron cryotomography to study membrane proteins across resolutions in native environments

Abstract:

Membrane proteins remain challenging targets for structural biology, despite much effort, as their native environment is heterogeneous and complex. Most methods rely on detergents to extract membrane proteins from their native environment, but this removal can significantly alter the structure and function of these proteins. Here, we overcome these challenges with a hybrid method to study membrane proteins in their native membranes, combining high-resolution solid-state nuclear magnetic reson...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1016/j.str.2017.11.011

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
ORCID:
0000-0001-9578-4263
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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM; Human Genetics Wt Centre
Role:
Author
ORCID:
0000-0002-8126-1979
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Funding agency for:
Baker, L
Grant:
Postdoctoral Fellowship
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Funding agency for:
Baker, L
Grant:
Postdoctoral Fellowship
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Funding agency for:
Grünewald, K
Grant:
Senior Research Fellowship (090895/Z/09/Z
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Grant:
Horizon 2020 program
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Publisher:
Cell Press Publisher's website
Journal:
Structure Journal website
Volume:
26
Issue:
1
Pages:
161-170.e3
Publication date:
2017-12-14
Acceptance date:
2017-11-15
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
Pmid:
29249608
Language:
English
Keywords:
Pubs id:
pubs:813191
UUID:
uuid:0d5344b8-4fde-4ff2-b7a7-3d81f5e584dc
Local pid:
pubs:813191
Deposit date:
2018-09-11

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