Crystallization and preliminary crystallographic analysis of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli.
N-Acetylglucosamine 6-phosphate deacetylase (E.C. 3.5.1.25), an enzyme from Escherichia coli involved in aminosugar catabolism, has been crystallized by the vapour-diffusion technique using phosphate as precipitant. X-ray diffraction experiments show the crystals to belong to the orthorhombic crystal system, with space group P2(1)2(1)2. The unit-cell parameters are a = 82.09 (2), b = 114.50 (1), c = 80.17 (1) A. The crystals diffract to a maximum resolution of 1.8 A and an initial data set was collected to 2.0 A.
Ferreira
F M
FM
Laboratório de Cristalografia de Proteínas e Biologia Estrutural, Instituto de Física de São Carlos, Universidade de São Paulo, Av. Dr Carlos Botelho 1465, Caixa Postal 369, 13560--970 São Carlos SP, Brazil.
Mendoza-Hernández
G
G
Calcagno
M L
ML
Minauro
F
F
Delboni
L F
LF
Oliva
G
G
D000581:Amidohydrolases / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D004926:Escherichia coli / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D011994:Recombinant Proteins; D000581:Amidohydrolases; C018717:N-acetylglucosamine-6-phosphate deacetylase