Overcoming barriers to membrane protein structure determination

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

Research output: Contribution to journalArticle

Abstract

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.
Original languageEnglish
Pages (from-to)335-340
Number of pages6
JournalNature Biotechnology
Volume29
Issue number4
DOIs
Publication statusPublished - 8 Apr 2011

Keywords

  • crystallization
  • protein databases
  • membrane proteins
  • protein engineering
  • protein stability
  • tertiary protein structure
  • protein unfolding
  • recombinant proteins
  • X-ray diffraction

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    Bill, R. M., Henderson, P. J. F., Iwata, S., Kunji, E. R. S., Michel, H., Neutze, R., Newstead, S., Poolman, B., Tate, C. G., & Vogel, H. (2011). Overcoming barriers to membrane protein structure determination. Nature Biotechnology, 29(4), 335-340. https://doi.org/10.1038/nbt.1833