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


The electron crystallographic structure of the aquaporin-1 water channel, determined at approximately 6A, reveals that the protein has six transmembrane alpha-helices 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 alpha-helix. 
DOI: 10.1038/nsb0497-263