Purification, Crystallization And Preliminary X-Ray Studies Of A P- Nitrophenylphosphatase From Bacillus Stearothermophilus

Authors: Ji C-N.1; Tian L.1; Feng C-J.1; Yin G.1; Shu G.1; Li J-X.1; Gong W-M.1; Pang H.1; Xie Y.1; Mao Y-M.1

Source: Protein and Peptide Letters, Volume 10, Number 5, October 2003 , pp. 521-524(4)

Publisher: Bentham Science Publishers

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Abstract:

Thermostable p-nitrophenylphosphatase from Bacillus stearothermophilus has been expressed in Escherichia coli, purified and crystallized. The crystals belong to space group C2, with unit-cell parameters a = 67.17 Å, b = 57.84 Å, c = 62.49 Å and agr = 90.0°, bgr = 95.4°, ggr = 90.0°. Diffraction data were collected to 1.40 Å resolution with a completeness of 94.7% (96.6% for the last shell), an Rfac value of 0.074 (0.341) and an I / sgr (I) value of 30.1 (2.67).

Keywords: crystallization; preliminary x-ray studies; thermostable p-nitrophenylphosphatase

Document Type: Review article

DOI: 10.2174/0929866033478708

Affiliations: 1: State Key Laboratory of Genetic Engineering, Institute of Genetics, Fudan University, Shanghai, 200433, People's Republic of China

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