Purification, crystallization and preliminary X-ray analysis of the peptidoglycan N-acetylglucosamine deacetylase BC1960 from Bacillus cereus in the presence of its substrate (GlcNAc){sub 6}
- Department of Biology, University of Crete, PO Box 2208, GR-71110, Heraklion, Crete (Greece)
- Institute of Molecular Biology and Biotechnology (IMBB), PO Box 1527, GR-71110, Heraklion, Crete (Greece)
The peptidoglycan N-acetylglucosamine (GlcNAc) deacetylase BC1960 from B. cereus was crystallized in the presence of the substrate (GlcNAc){sub 6}. The crystals belonged to space group P4{sub 1}2{sub 1}2 and diffracted to 2.38 Å resolution. The peptidoglycan N-acetylglucosamine (GlcNAc) deacetylase BC1960 from Bacillus cereus (EC 3.5.1.33), an enzyme consisting of 275 amino acids, was crystallized in the presence of its substrate (GlcNAc){sub 6}. The crystals belonged to the tetragonal space group P4{sub 1}2{sub 1}2, with unit-cell parameters a = b = 92.7, c = 242.9 Å and four molecules in the asymmetric unit. A complete data set was collected at 100 K to a resolution of 2.38 Å using synchrotron radiation.
- OSTI ID:
- 22360475
- Journal Information:
- Acta Crystallographica. Section F, Vol. 64, Issue Pt 3; Other Information: PMCID: PMC2374148; PMID: 18323609; PUBLISHER-ID: bw5221; OAI: oai:pubmedcentral.nih.gov:2374148; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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