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

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

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

Publisher: Bentham Science Publishers

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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

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866033478708

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

Publication date: October 1, 2003

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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