title: Preliminary crystallization and X-ray analysis of orthorhombic human endothelin.
abstract: Human endothelin (ET-1) is a highly potent, ubiquitous, endogenous 21 amino acid residue polypeptide, which acts as a vaso- and bronchoconstrictor. Crystals of the active, uncomplexed form of ET-1 have been grown from aqueous solutions. These crystals, which are long hexagonal prisms, diffract to 2.98 A and are apparently of the space group P222(1) with cell dimensions a = 33.5 A, b = 57.9 A, c = 59.6 A. The six molecules in the asymmetric unit are related by non-crystallographic symmetry operations, which result in a pseudo 6(1) appearance to the data.
authors.affiliation: Department of Crystallography, Birkbeck College University of London, U.K.
authors.forename: D H
authors.initials: DH
authors.lastname: Peapus
authors.forename: R W
authors.initials: RW
authors.lastname: Janes
authors.forename: B A
authors.initials: BA
authors.lastname: Wallace
mesh_terms: D018360:Crystallography, X-Ray; D016232:Endothelins; D006801:Humans
chemical_list: D016232:Endothelins