title: Preliminary crystallographic study of peanut peroxidase.
abstract: The cationic isozyme of peroxidase isolated from suspension cultures of peanut cells is a heme-containing and calcium-dependent glycoprotein having four covalently attached oligosaccharide chains. Attempts were made to crystallize the glycoprotein for X-ray diffraction analysis, and these have met with some success. Crystals have now been grown that are suitable for a full three-dimensional structural analysis. The crystals are thin plates and we have shown them to be of the orthorhombic space group P2(1)2(1)2(1) with a = 48.1, b = 97.2, c = 146.2 A. The crystals diffract to beyond 2.8 A resolution, appear to be stable to lengthy X-ray exposure, and contain two molecules of 40,000 daltons each in the asymmetric unit.
authors.affiliation: Department of Biochemistry, University of California, Riverside 92521.
authors.forename: N
authors.initials: N
authors.lastname: Ban
authors.forename: R B
authors.initials: RB
authors.lastname: van Huystee
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: R
authors.initials: R
authors.lastname: Esnault
authors.forename: A
authors.initials: A
authors.lastname: McPherson
mesh_terms: D010367:Arachis / Q000201:enzymology*; D003460:Crystallization; D007527:Isoenzymes / Q000737:chemistry*; D010544:Peroxidases / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D007527:Isoenzymes; D010544:Peroxidases