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

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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


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

Publication date: 2003-10-01

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