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research article

Overcoming barriers to membrane protein structure determination

Bill, Roslyn M.
•
Henderson, Peter J. F.
•
Iwata, So
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2011
Nature Biotechnology

After decades of slow progress, the pace of research on membrane protein structures is beginning to quicken thanks to various improvements in technology, including protein engineering and microfocus X-ray diffraction. Here we review these developments and, where possible, highlight generic new approaches to solving membrane protein structures based on recent technological advances. Rational approaches to overcoming the bottlenecks in the field are urgently required as membrane proteins, which typically comprise similar to 30% of the proteomes of organisms, are dramatically under-represented in the structural database of the Protein Data Bank.

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Type
research article
DOI
10.1038/nbt.1833
Web of Science ID

WOS:000289284900018

Author(s)
Bill, Roslyn M.
Henderson, Peter J. F.
Iwata, So
Kunji, Edmund R. S.
Michel, Hartmut
Neutze, Richard
Newstead, Simon
Poolman, Bert
Tate, Christopher G.
Vogel, Horst  
Date Issued

2011

Published in
Nature Biotechnology
Volume

29

Issue

4

Start page

335

End page

340

Subjects

Size-Exclusion Chromatography

•

Hydantoin Transporter Mhp1

•

X-Ray Crystallography

•

Cytochrome-C-Oxidase

•

Crystal-Structure

•

Coupled Receptor

•

Escherichia-Coli

•

Lactococcus-Lactis

•

Molecular-Basis

•

Angstrom Resolution

Editorial or Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
LCPPM  
Available on Infoscience
May 3, 2011
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/66993
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