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

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

Volume: 10 Issue: 5

Author(s): Chao-Neng Ji, Liang Tian, Cong-Jing Feng, Gang Yin, Guang Shu, Ji-Xi Li, Wei-Ming Gong, Hai Pang, Yi Xie and Yu-Min Mao

Affiliation:

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

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).

Cite this article as:

Ji Chao-Neng, Tian Liang, Feng Cong-Jing, Yin Gang, Shu Guang, Li Ji-Xi, Gong Wei-Ming, Pang Hai, Xie Yi and Mao Yu-Min, Purification, Crystallization And Preliminary X-Ray Studies Of A P- Nitrophenylphosphatase From Bacillus Stearothermophilus, Protein & Peptide Letters 2003; 10 (5) . https://dx.doi.org/10.2174/0929866033478708