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Published on: December 30, 2016
Purification, crystallization and preliminary X-ray studies of a p-nitrophenylphosphatase from Bacillus
Chao-Neng Ji1, Liang Tian, Cong-Jing Feng
1State Key Laboratory of Genetic Engineering, Institute of Genetics, Fudan University, Shanghai, 200433, People's Republic of China.
Abstract:
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).
