Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 3 (March 2008)

crystallization communications


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Acta Cryst. (2008). F64, 203-205    [ doi:10.1107/S1744309108002510 ]

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

A. Tsalafouta, E. Psylinakis, E. G. Kapetaniou, D. Kotsifaki, A. Deli, A. Roidis, V. Bouriotis and M. Kokkinidis

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 P41212, 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.

Keywords: N-acetylglucosamine deacetylases; peptidoglycan modification.

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