PMID:10771446
| Citation |
Ferreira, FM, Mendoza-Hernández, G, Calcagno, ML, Minauro, F, Delboni, LF and Oliva, G (2000) Crystallization and preliminary crystallographic analysis of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 56:670-2 |
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| Abstract |
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. |
| Links | |
| Keywords |
Amidohydrolases/chemistry; Amidohydrolases/isolation & purification; Crystallization; Crystallography, X-Ray/methods; Escherichia coli/enzymology; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification |
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