Crystallization and preliminary analysis of chondroitinase AC from 
Flavobacterium heparinum

Féthière, James; Shilton, B.; Li, Y.; Laliberté, M.; Eggimann, Bernhard; Cygler, Miroslaw

doi:10.1107/S0907444997009037

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Crystallization and preliminary analysis of chondroitinase AC from Flavobacterium heparinum

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Féthière, James
Max Planck Research Group Ion Channel Structure (Dean R. Madden), Max Planck Institute for Medical Research, Max Planck Society;

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http://journals.iucr.org/d/issues/1998/02/00/gr0744/gr0744.pdf
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Citation

Féthière, J., Shilton, B., Li, Y., Laliberté, M., Eggimann, B., & Cygler, M. (1998). Crystallization and preliminary analysis of chondroitinase AC from Flavobacterium heparinum. Acta Crystallographica Section D: Structural Biology, 54(2), 279-280. doi:10.1107/S0907444997009037.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002B-9B9A-8

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.