Ferreira F M, Mendoza-Hernández G, Calcagno M L, Minauro F, Delboni L F, Oliva G
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.
Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):670-2. doi: 10.1107/s0907444900003668.
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.
N-乙酰葡糖胺6-磷酸脱乙酰酶（E.C. 3.5.1.25）是一种来自大肠杆菌、参与氨基糖分解代谢的酶，已通过气相扩散技术以磷酸盐作为沉淀剂进行了结晶。X射线衍射实验表明，这些晶体属于正交晶系，空间群为P2(1)2(1)2。晶胞参数为a = 82.09 (2)，b = 114.50 (1)，c = 80.17 (1) Å。这些晶体的衍射极限分辨率为1.8 Å，并收集了至2.0 Å的初始数据集。
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