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Purification, crystallization and preliminary X-ray analysis of the peptidoglycan N-acetylglucosamine deacetylase BC1960 from Bacillus cereus in the presence of its substrate (GlcNAc)6.

Authors
Type
Published Article
Journal
Acta Crystallographica Section F Structural Biology and Crystallization Communications
1744-3091
Publisher
International Union of Crystallography
Publication Date
Volume
64
Issue
Pt 3
Pages
203–205
Identifiers
DOI: 10.1107/S1744309108002510
PMID: 18323609
Source
Medline
License
Unknown

Abstract

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)(6). The crystals belonged to the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 92.7, c = 242.9 A and four molecules in the asymmetric unit. A complete data set was collected at 100 K to a resolution of 2.38 A using synchrotron radiation.

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