Crystallization and preliminary analysis of chondroitinase AC from Flavobacterium heparinum

被引：8

作者：

Fethiere, J

Shilton, BH

Li, YG

Allaire, M

Laliberte, M

Eggimann, B

Cygler, M

机构：

[1] Natl Res Council Canada, Biotechnol Res Inst, Montreal, PQ H4P 2R2, Canada

[2] Ibex Technol, Montreal, PQ H4P 2R2, Canada

[3] Montreal Joint Ctr Struct Biol, Montreal, PQ, Canada

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1998年 / 54卷

关键词：

D O I：

10.1107/S0907444997009037

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

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 P4(3)2(1)2 or its enantiomorph with a = b = 87.1 and c = 193.1 Angstrom and one molecule in the asymmetric unit. Crystals diffract to a maximum of 2.5 Angstrom 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.

引用

页码：279 / 280

页数：2

共 16 条

[1] ENZYMATIC DEGRADATION OF GLYCOSAMINOGLYCANS [J].