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

Chao-Neng Ji; Liang Tian; Cong-Jing Feng; Gang Yin; Guang Shu; Ji-Xi Li; Wei-Ming Gong; Hai Pang; Yi Xie; Yu-Min Mao

doi:10.2174/0929866033478708

ISSN: 0929-8665
E-ISSN: 1875-5305

Purification, Crystallization And Preliminary X-Ray Studies Of A P- Nitrophenylphosphatase From Bacillus Stearothermophilus
Authors: Chao-Neng Ji¹, Liang Tian², Cong-Jing Feng³, Gang Yin⁴, Guang Shu⁵, Ji-Xi Li⁶, Wei-Ming Gong⁷, Hai Pang⁸, Yi Xie⁹ and Yu-Min Mao¹⁰
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¹ State Key Laboratory of Genetic Engineering, Institute of Genetics, Fudan University, Shanghai, 200433, People's Republic of China ² State Key Laboratory of Genetic Engineering, Institute of Genetics, Fudan University, Shanghai, 200433, People's Republic of China ³ State Key Laboratory of Genetic Engineering, Institute of Genetics, Fudan University, Shanghai, 200433, People's Republic of China ⁴ State Key Laboratory of Genetic Engineering, Institute of Genetics, Fudan University, Shanghai, 200433, People's Republic of China ⁵ State Key Laboratory of Genetic Engineering, Institute of Genetics, Fudan University, Shanghai, 200433, People's Republic of China ⁶ State Key Laboratory of Genetic Engineering, Institute of Genetics, Fudan University, Shanghai, 200433, People's Republic of China ⁷ State Key Laboratory of Genetic Engineering, Institute of Genetics, Fudan University, Shanghai, 200433, People's Republic of China ⁸ State Key Laboratory of Genetic Engineering, Institute of Genetics, Fudan University, Shanghai, 200433, People's Republic of China ⁹ State Key Laboratory of Genetic Engineering, Institute of Genetics, Fudan University, Shanghai, 200433, People's Republic of China ¹⁰ State Key Laboratory of Genetic Engineering, Institute of Genetics, Fudan University, Shanghai, 200433, People's Republic of China
Source: Protein and Peptide Letters, Volume 10, Issue 5, Oct 2003, p. 521 - 524
DOI: https://doi.org/10.2174/0929866033478708
- Available online: 01 Oct 2003

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 α = 90.0°, β = 95.4°, γ = 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 / σ (I) value of 30.1 (2.67).

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2003-10-01

2025-05-23

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Article Type: Review Article

Keyword(s): crystallization; preliminary x-ray studies; thermostable p-nitrophenylphosphatase

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

Abstract

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