Crystallization and preliminary analysis of chondroitinase AC from Flavobacterium heparinum

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 Å and one molecule in the asy...

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Veröffentlicht in:	Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1998-03, Vol.54 (2), p.279-280
Hauptverfasser:	Féthière, James, Shilton, Brian H., Li, Yunge, Allaire, Marc, Laliberté, Maryse, Eggimann, Bernhard, Cygler, Miroslaw
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Chondroitin Lyases - chemistry Chondroitin Lyases - isolation & purification Crystallization Crystallography, X-Ray Flavobacterium - enzymology Metals, Heavy
Online-Zugang:	Volltext
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Beschreibung
Zusammenfassung:	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 Å and one molecule in the asymmetric unit. Crystals diffract to a maximum of 2.5 Å 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.
ISSN:	1399-0047 0907-4449 1399-0047
DOI:	10.1107/S0907444997009037