title: The CHIP28 water channel visualized in ice by electron crystallography.
abstract: Electron crystallography of frozen-hydrated two-dimensional crystals of deglycosylated human erythrocyte CHIP28 reveals an aqueous vestibule in each monomer leading to the water-selective channel that is enclosed by multiple transmembrane alpha-helices.
authors.forename: A K
authors.initials: AK
authors.lastname: Mitra
authors.forename: A N
authors.initials: AN
authors.lastname: van Hoek
authors.forename: M C
authors.initials: MC
authors.lastname: Wiener
authors.forename: A S
authors.initials: AS
authors.lastname: Verkman
authors.forename: M
authors.initials: M
authors.lastname: Yeager
mesh_terms: D002463:Cell Membrane Permeability; D003461:Crystallography / Q000379:methods*; D004583:Electrons; D004912:Erythrocytes / Q000737:chemistry / Q000378:metabolism; D005615:Freezing; D006031:Glycosylation; D006801:Humans; D007473:Ion Channels / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary; D014867:Water / Q000378:metabolism*
chemical_list: D007473:Ion Channels; D014867:Water