title: Crystallization and preliminary X-ray analysis of chondroitinase B from Flavobacterium heparinum.
abstract: Chondroitinase B, a glycosaminoglycan lyase from Flavobacterium heparinum, has been crystallized by hanging-drop vapor diffusion in space group P21 with unit-cell parameters a = 50.6, b = 74.5, c = 58. 7 A, beta = 92.9 degrees and one molecule in the asymmetric unit. This enzyme degrades dermatan sulfate, a glycosaminoglycan primarily made up of a disaccharide repeating unit of iduronic acid and N-acetylgalactosamine. A complete native data set has been collected from a single crystal to 2.2 A resolution using a rotating-anode source.
authors.affiliation: Biotechnology Research Institute, 6100 Royalmount Ave., Montreal, QC, Canada H4P 2R2 and Montreal Joint Center for Structural Biology, Montreal, QC, Canada.
authors.forename: Y
authors.initials: Y
authors.lastname: Li
authors.forename: A
authors.initials: A
authors.lastname: Matte
authors.forename: H
authors.initials: H
authors.lastname: Su
authors.forename: M
authors.initials: M
authors.lastname: Cygler
mesh_terms: D019765:Chondroitin ABC Lyase / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D005417:Flavobacterium / Q000201:enzymology*
chemical_list: D019765:Chondroitin ABC Lyase