- Crystallization and preliminary analysis of chondroitinase AC from Flavobacterium heparinum.
Crystallization and preliminary analysis of chondroitinase AC from Flavobacterium heparinum.
Acta crystallographica. Section D, Biological crystallography (1998-10-08)
J Féthière, B H Shilton, Y Li, M Allaire, M Laliberté, B Eggimann, M Cygler
PMID9761894
ABSTRACT
Chondroitinase AC (E.C. 4.2.2.5) overexpressed in its host, Flavobacterium heparinum, was crystallized by vapor diffusion using polyethylene glycol methyl ether as precipitant. It crystallizes in the space group P43212 or its enantiomorph with a = b = 87.1 and c = 193.1 A and one molecule in the asymmetric unit. Crystals diffract to a maximum of 2.5 A resolution on a rotating-anode source. Screening for heavy-atom derivatives identified a lead compound that binds to a single site on the protein. Further screening is in progress.
MATERIALS
Product Number
Brand
Product Description
Sigma-Aldrich
Chondroitinase AC from Flavobacterium heparinum, lyophilized powder, 0.5-1.5 units/mg protein (using chondroitin sulfate A as substrate)
Sigma-Aldrich
Chondroitinase AC from Flavobacterium heparinum, recombinant, expressed in E. coli, ≥200 units/mg protein, For Chondroitin Sulfate Analysis