Crystallization and preliminary crystallographic analysis of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli

被引:7
作者
Ferreira, FM
Mendoza-Hernámdez, G
Calcagno, ML
Minauro, F
Delboni, LF
Oliva, G
机构
[1] Univ Sao Paulo, Inst Fis Sao Carlos, Lab Cristalog Prot & Biol Estrutural, BR-13560970 Sao Carlos, SP, Brazil
[2] Univ Nacl Autonoma Mexico, Fac Med, Dept Bioquim, Mexico City 04510, DF, Mexico
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2000年 / 56卷
关键词
D O I
10.1107/S0907444900003668
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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) Angstrom. The crystals diffract to a maximum resolution of 1.8 Angstrom and an initial data set was collected to 2.0 Angstrom.
引用
收藏
页码:670 / 672
页数:3
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