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  Crystallization and preliminary analysis of chondroitinase AC from Flavobacterium heparinum

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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-9B9A-8 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-9BA1-5
Genre: Journal Article
Alternative Title : Preliminary crystallographic analysis of chondroitinase AC from Flavobacterium heparinum

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ActaCrystD_54_1998_279.pdf (Any fulltext), 758KB
 
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http://journals.iucr.org/d/issues/1998/02/00/gr0744/gr0744.pdf (Any fulltext)
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 Creators:
Féthière, James1, Author           
Shilton, B., Author
Li, Y., Author
Laliberté, M., Author
Eggimann, Bernhard, Author
Cygler, Miroslaw, Author
Affiliations:
1Max Planck Research Group Ion Channel Structure (Dean R. Madden), Max Planck Institute for Medical Research, Max Planck Society, ou_1497725              

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 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.

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Language(s): eng - English
 Dates: 1997-03-311997-06-171998-03-01
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 666653
DOI: 10.1107/S0907444997009037
URI: https://www.ncbi.nlm.nih.gov/pubmed/9761894
URI: http://scripts.iucr.org/cgi-bin/paper?S0907444997009037
Other: 4288
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Title: Acta Crystallographica Section D: Structural Biology
  Abbreviation : Acta Cryst. D
Source Genre: Journal
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Publ. Info: Chester, England : International Union of Crystallography
Pages: - Volume / Issue: 54 (2) Sequence Number: - Start / End Page: 279 - 280 Identifier: ISSN: 2059-7983
CoNE: https://pure.mpg.de/cone/journals/resource/2059-7983