Overcoming barriers to membrane protein structure determination

Bill, Roslyn M., Henderson, Peter J.F., Iwata, So, Kunji, Edmund R.S., Michel, Hartmut, Neutze, Richard, Newstead, Simon, Poolman, Bert, Tate, Christopher G. and Vogel, Horst (2011). Overcoming barriers to membrane protein structure determination. Nature Biotechnology, 29 (4), pp. 335-340.


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 ~30% of the proteomes of organisms, are dramatically under-represented in the structural database of the Protein Data Bank.

Publication DOI: https://doi.org/10.1038/nbt.1833
Divisions: Life & Health Sciences
Life & Health Sciences > Biosciences
Uncontrolled Keywords: crystallization,protein databases,membrane proteins,protein engineering,protein stability,tertiary protein structure,protein unfolding,recombinant proteins,X-ray diffraction,Applied Microbiology and Biotechnology,Biotechnology,Molecular Medicine,Bioengineering,Biomedical Engineering
Full Text Link: http://www.natu ... l/nbt.1833.html
Related URLs: http://www.scop ... tnerID=8YFLogxK (Scopus URL)
Published Date: 2011-04-08
Authors: Bill, Roslyn M. ( 0000-0003-1331-0852)
Henderson, Peter J.F.
Iwata, So
Kunji, Edmund R.S.
Michel, Hartmut
Neutze, Richard
Newstead, Simon
Poolman, Bert
Tate, Christopher G.
Vogel, Horst



Version: Accepted Version

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