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Molecular design of aquaporin-1 water channel as revealed by electron crystallography

Nature Structural Biology volume 4, pages 263–265 (1997)Cite this article

The electron crystallographic structure of the aquaporin-1 water channel, determined at ∼6Å, reveals that the protein has six transmembrane αhelices forming a trapezoid-like cylinder. There is a branched rod-like structure within the cylinder that traverses the membrane and likely contains at least one α-helix.

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Authors and Affiliations

  1. Life Sciences Division, Lawrence Berkeley National Laboratory, University of California, Berkeley, CA, 94720, USA

    Huilin Li, Susan Lee & Bing K. Jap

  2. Life Sciences Division, Lawrence Berkeley National Laboratory, University of California, Berkeley, CA, 94720, USA

    Bing K. Jap

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  1. Huilin Li
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  2. Susan Lee
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  3. Bing K. Jap
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Li, H., Lee, S. & Jap, B. Molecular design of aquaporin-1 water channel as revealed by electron crystallography. Nat Struct Mol Biol 4, 263–265 (1997). https://doi.org/10.1038/nsb0497-263

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