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

Author(s): 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.

Journal Name: Protein & Peptide Letters

Volume 10 , Issue 5 , 2003

Become EABM
Become Reviewer

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).

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

Rights & PermissionsPrintExport Cite as


Article Details

VOLUME: 10
ISSUE: 5
Year: 2003
Page: [521 - 524]
Pages: 4
DOI: 10.2174/0929866033478708
Price: $58

Article Metrics

PDF: 2