嗜热脂肪芽孢杆菌对硝基苯磷酸酶的纯化、结晶及初步X射线研究
Purification, crystallization and preliminary X-ray studies of a p-nitrophenylphosphatase from Bacillus stearothermophilus.
作者信息
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
机构信息
State Key Laboratory of Genetic Engineering, Institute of Genetics, Fudan University, Shanghai, 200433, People's Republic of China.
出版信息
Protein Pept Lett. 2003 Oct;10(5):521-4. doi: 10.2174/0929866033478708.
Thermostable p-nitrophenylphosphatase from Bacillus stearothermophilus has been expressed in Escherichia coli, purified and crystallized. The crystals belong to space group C(2), with unit-cell parameters a = 67.17 A, b = 57.84 A, c = 62.49 A and alpha = 90.0 degrees, beta = 95.4 degrees, gamma = 90.0 degrees. Diffraction data were collected to 1.40 A resolution with a completeness of 94.7% (96.6% for the last shell), an R(fac) value of 0.074 (0.341) and an I/sigma (I) value of 30.1 (2.67).
嗜热脂肪芽孢杆菌的耐热对硝基苯磷酸酶已在大肠杆菌中表达、纯化并结晶。晶体属于空间群C(2)，晶胞参数为a = 67.17 Å，b = 57.84 Å，c = 62.49 Å，α = 90.0°，β = 95.4°，γ = 90.0°。衍射数据收集至1.40 Å分辨率，完整性为94.7%（最后一层为96.6%），R(fac)值为0.074（0.341），I/σ(I)值为30.1（2.67）。
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