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Projection structure of a ClC-type chloride channel at 6.5 Å resolution

Author

Listed:
  • Joseph A. Mindell

    (Howard Hughes Medical Institute)

  • Merritt Maduke

    (Howard Hughes Medical Institute)

  • Christopher Miller

    (Howard Hughes Medical Institute)

  • Nikolaus Grigorieff

    (Howard Hughes Medical Institute
    Rosenstiel Basic Medical Science Research Center and W. M. Keck Institute for Cellular Visualization, Brandeis University)

Abstract

Virtually all cells in all eukaryotic organisms express ion channels of the ClC type, the only known molecular family of chloride-ion-selective channels. The diversity of ClC channels highlights the multitude and range of functions served by gated chloride-ion conduction in biological membranes, such as controlling electrical excitability in skeletal muscle, maintaining systemic blood pressure, acidifying endosomal compartments, and regulating electrical responses of GABA (γ-aminobutyric acid)-containing interneurons in the central nervous system1. Previously, we expressed and purified a prokaryotic ClC channel homologue2. Here we report the formation of two-dimensional crystals of this ClC channel protein reconstituted into phospholipid bilayer membranes. Cryo-electron microscopic analysis of these crystals yields a projection structure at 6.5 Å resolution, which shows off-axis water-filled pores within the dimeric channel complex.

Suggested Citation

  • Joseph A. Mindell & Merritt Maduke & Christopher Miller & Nikolaus Grigorieff, 2001. "Projection structure of a ClC-type chloride channel at 6.5 Å resolution," Nature, Nature, vol. 409(6817), pages 219-223, January.
    • Handle: RePEc:nat:nature:v:409:y:2001:i:6817:d:10.1038_35051631
    DOI: 10.1038/35051631
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