title: Preliminary X-ray crystallographic study of cyanase from Escherichia coli.
abstract: Cyanase, an oligomeric enzyme of Escherichia coli that catalyzes the decomposition of cyanate to ammonia and bicarbonate, crystallizes in the space group P1 with unit cell parameters a = 85.96 A, b = 83.17 A, c = 83.28 A, alpha = 110.29 degrees, beta = 118.29 degrees and gamma = 72.40 degrees. Crystals diffract to a resolution of at least 2.5 A. The crystal data, in conjunction with a subunit molecular weight of 17,008, suggest that two oligomers are in the asymmetric unit of the crystal and that eight subunits comprise a single oligomer.
authors.affiliation: Department of Biochemistry and Biophysics, Iowa State University, Ames 50011.
authors.forename: K H
authors.initials: KH
authors.lastname: Kim
authors.forename: R B
authors.initials: RB
authors.lastname: Honzatko
authors.forename: R M
authors.initials: RM
authors.lastname: Little
authors.forename: P M
authors.initials: PM
authors.lastname: Anderson
mesh_terms: D000619:Aminohydrolases; D019759:Carbon-Nitrogen Lyases; D004926:Escherichia coli / Q000201:enzymology*; D008970:Molecular Weight; D014961:X-Ray Diffraction
chemical_list: D000619:Aminohydrolases; C019953:cyanate hydrolase; D019759:Carbon-Nitrogen Lyases