Crystallization and preliminary X-ray analysis of chondroitin sulfate ABC lyases I and II from Proteus vulgaris

Chondroitin sulfate ABC lyases (E.C. 4.2.2.4) are broad-specificity glycosa minoglycan-degrading enzymes. Their preferred substrates are chondroitin su lfate and dermatan sulfate, which are broken down to short oligosaccharides . Proteus vulgaris produces two such lyases, ABC lyase I and II, with molec ular weights of 112-113 kDa. Diffraction-quality crystals of both enzymes h ave been obtained by the hanging-drop vapour-diffusion method. ABC lyase I crystallizes in space group P2(1)2(1)2(1), with unit-cell parameters a = 49 .3, b = 95.1, c = 230.0 Angstrom, Z = 4, and diffracts to 1.9 Angstrom reso lution. Crystals of ABC lyase II belong to space group P1, with unit-cell p arameters a = 64.2, b = 64.3, c = 142.1 Angstrom, alpha = 95.7, beta = 98.1 , gamma = 95.5 degrees, Z = 2; diffraction extends to at least 2.1 Angstrom .