Crystallization and preliminary X-ray analysis of chondroitinase B from Flavobacterium heparinum

Citation
Yg. Li et al., Crystallization and preliminary X-ray analysis of chondroitinase B from Flavobacterium heparinum, ACT CRYST D, 55, 1999, pp. 1055-1057
Citations number
18
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
55
Year of publication
1999
Part
5
Pages
1055 - 1057
Database
ISI
SICI code
0907-4449(199905)55:<1055:CAPXAO>2.0.ZU;2-F
Abstract
Chondroitinase B, a glycosaminoglycan lyase from Flavobacterium heparinum, has been crystallized by hanging-drop vapor diffusion in space group P2(1) with unit-cell parameters a = 50.6, b = 74.5, c= 58.7 Angstrom, beta = 92.9 degrees and one molecule in the asymmetric unit. This enzyme degrades derm atan sulfate, a glycosaminoglycan primarily made up of a disaccharide repea ting unit of iduronic acid and N-acetylgalactosamine, A complete native dat a set has been collected from a single crystal to 2.2 Angstrom resolution u sing a rotating-anode source.