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Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy

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  • Liguo Wang

    (Yale University, 333 Cedar Street, New Haven, Connecticut 06520, USA)

  • Fred J. Sigworth

    (Yale University, 333 Cedar Street, New Haven, Connecticut 06520, USA)

Abstract

Membrane proteins: structures without crystallization Here the authors report the structure of a membrane protein, the human large-conductance calcium- and voltage-activated potassium (BK) channel, in its native membrane environment using single-particle electron cryomicroscopy. From images of 8,400 individual protein particles, a three-dimensional reconstruction of the BK channel was obtained at a resolution of 17–20 Å. The disposition of the voltage-sensor domains of the 6TM channels has been a matter of controversy, but these authors find that the membrane-embedded channel's voltage-sensor domains match well with two recent 6TM channel X-ray crystal structures. Since this method does not require the formation of crystals, it is likely to be useful in the structural studies of other membrane proteins in their native membrane environment.

Suggested Citation

  • Liguo Wang & Fred J. Sigworth, 2009. "Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy," Nature, Nature, vol. 461(7261), pages 292-295, September.
    • Handle: RePEc:nat:nature:v:461:y:2009:i:7261:d:10.1038_nature08291
    DOI: 10.1038/nature08291
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    Cited by:

    1. Wendy L Imlach & Sarah C Finch & John H Miller & Andrea L Meredith & Julie E Dalziel, 2010. "A Role for BK Channels in Heart Rate Regulation in Rodents," PLOS ONE, Public Library of Science, vol. 5(1), pages 1-7, January.

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