Purification, crystallization and preliminary X-ray studies of a p-nitrophenylphosphatase from Bacillus stearothermophilus.
Thermostable p-nitrophenylphosphatase from Bacillus stearothermophilus has been expressed in Escherichia coli, purified and crystallized. The crystals belong to space group C(2), with unit-cell parameters a = 67.17 A, b = 57.84 A, c = 62.49 A and alpha = 90.0 degrees, beta = 95.4 degrees, gamma = 90.0 degrees. Diffraction data were collected to 1.40 A resolution with a completeness of 94.7% (96.6% for the last shell), an R(fac) value of 0.074 (0.341) and an I/sigma (I) value of 30.1 (2.67).
Ji
Chao-Neng
CN
State Key Laboratory of Genetic Engineering, Institute of Genetics, Fudan University, Shanghai, 200433, People's Republic of China.
Tian
Liang
L
Feng
Cong-Jing
CJ
Yin
Gang
G
Shu
Guang
G
Li
Ji-Xi
JX
Gong
Wei-Ming
WM
Pang
Hai
H
Xie
Yi
Y
Mao
Yu-Min
YM
D009597:4-Nitrophenylphosphatase / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000706:statistics & numerical data; D001411:Geobacillus stearothermophilus / Q000201:enzymology*
D009597:4-Nitrophenylphosphatase