title: Crystallization and preliminary X-ray analysis of human endothelin.
abstract: Endothelin, a potent regulator of vasoconstriction and hypertension, is a naturally produced peptide of 21 amino acids containing two disulfide bonds. We have crystallized endothelin from humans using the vapor-diffusion technique, characterized the crystals by X-ray diffraction analysis, and have collected the X-ray intensities to a resolution of 1.8 A. The crystals, which demonstrate physical properties similar to most protein crystals and have a comparable solvent content, are hexagonal prisms that frequently grow to lengths of 400 microns and widths of 150 microns. The space group of the crystals is P6(1)22 (or P6(5)22), with a = 27.4, c = 79.6 A. There is one molecule of endothelin in the asymmetric unit of the crystals.
authors.affiliation: Department of Biochemistry, University of California, Riverside 92521.
authors.forename: M
authors.initials: M
authors.lastname: Wolff
authors.forename: J
authors.initials: J
authors.lastname: Day
authors.forename: A
authors.initials: A
authors.lastname: Greenwood
authors.forename: S
authors.initials: S
authors.lastname: Larson
authors.forename: A
authors.initials: A
authors.lastname: McPherson
mesh_terms: D003460:Crystallization; D016232:Endothelins / Q000138:chemical synthesis / Q000737:chemistry*; D006801:Humans; D011487:Protein Conformation; D014961:X-Ray Diffraction / Q000379:methods
chemical_list: D016232:Endothelins