Crystallization and preliminary X-ray analysis of chondroitinase B from Flavobacterium heparinum.
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.
Li
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Biotechnology Research Institute, 6100 Royalmount Ave., Montreal, QC, Canada H4P 2R2 and Montreal Joint Center for Structural Biology, Montreal, QC, Canada.
Matte
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Su
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Cygler
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D019765:Chondroitin ABC Lyase / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D005417:Flavobacterium / Q000201:enzymology*
D019765:Chondroitin ABC Lyase