Open AccessPurification, crystallization and preliminary X‐ray analysis of the peptidoglycan N ‐acetylglucosamine deacetylase BC1960 from Bacillus cereus in the presence of its substrate (GlcNAc) 6
Author(s) -
Tsalafouta Aleka,
Psylinakis Emmanuel,
Kapetaniou Evangelia G.,
Kotsifaki Dina,
Deli Alexandra,
Roidis Alexandros,
Bouriotis Vasilis,
Kokkinidis Michael
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108002510
Subject(s) - bacillus cereus , peptidoglycan , tetragonal crystal system , crystallization , substrate (aquarium) , cereus , chemistry , n acetylglucosamine , resolution (logic) , crystallography , stereochemistry , cell wall , bacteria , enzyme , biochemistry , biology , crystal structure , organic chemistry , ecology , genetics , artificial intelligence , computer science
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 P 4 1 2 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.