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  • 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
摘要

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.

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Sigma-Aldrich
软骨素酶AC 来源于肝素黄杆菌, recombinant, expressed in E. coli, ≥200 units/mg protein, For Chondroitin Sulfate Analysis
Sigma-Aldrich
软骨素酶AC 来源于肝素黄杆菌, lyophilized powder, 0.5-1.5 units/mg protein (using chondroitin sulfate A as substrate)