title: Crystallization and preliminary X-ray diffraction study of the heat-labile enterotoxin B subunit produced by enterotoxigenic Escherichia coli.
abstract: Heat-labile enterotoxin LT produced by enterotoxigenic Escherichia coli is composed of A and B subunits. The A subunit is enzymatically active; whereas, through the action of the B subunit, the toxin binds to the receptor, a GM1 ganglioside present on the cell surface. Crystals of the LT-B subunit were formed at room temperature by vapor diffusion with polyethylene glycol in the presence of the non-ionic detergent beta-octylglucoside. The crystals were characterized by X-radiation as orthorhombic, space group P2(1)2(1)2(1), with unit cell dimensions of a = 224.1 A, b = 65.3 A, c = 118.4 A. They diffract X-rays to a resolution of at least 2.5 A and are stable to X-rays.
authors.affiliation: Department of Bacteriology and Serology, Osaka University, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Tsuji
authors.forename: K
authors.initials: K
authors.lastname: Fukuyama
authors.forename: H
authors.initials: H
authors.lastname: Matsubara
authors.forename: T
authors.initials: T
authors.lastname: Honda
authors.forename: T
authors.initials: T
authors.lastname: Miwatani
mesh_terms: D001427:Bacterial Toxins; D003460:Crystallization; D004768:Enterotoxins; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D014961:X-Ray Diffraction
chemical_list: D001427:Bacterial Toxins; D004768:Enterotoxins; D029968:Escherichia coli Proteins; C027538:heat-labile enterotoxin, E coli