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 | Zendy

Tsalafouta Aleka | Zendy; Psylinakis Emmanuel | Zendy; Kapetaniou Evangelia G. | Zendy; Kotsifaki Dina | Zendy; Deli Alexandra | Zendy; Roidis Alexandros | Zendy; Bouriotis Vasilis | Zendy; Kokkinidis Michael | Zendy

Open Access

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

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research