Lipid protein interactions in double layered two-dimensional AQPO crystals
Article Abstract:
The lens specific aquaporin-O (AQPO) functions as a specific water pore and forms the thin junctions between fibre cells. The resolution structure of junctional AQPO is described and determined by electron crystallography of double layered two-dimensional crystals, which shows that the packing interactions between AQPO tetramers in the crystalline array are mediated by lipid molecules.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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Molecular model for a complete clathrin lattice from electron cryomicroscopy
Article Abstract:
A report on the structure of a clathrin lattice at subnanometre resolution, obtained from electron cryomicroscopy of coats assembled in vitro is presented. It concluded that analysis of coats with distinct diameters show an invariant pattern of contacts in the neighborhood of each vertex, with more variable interactions along the extended parts of the triskelion 'legs'.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2004
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Aquaporin-0 membrane junctions reveal the structure of a closed water pore
Article Abstract:
The lens-specific water pore aquaporin-0 (AQP0) is the only aquaporin known to from membrane junctions in vivo. The structure of the AQP0 membrane junction as determined by electron crystalography is presented.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2004
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