Purification, crystallization and preliminary X-ray studies of thermostable alkaline phosphatase from Thermus sp. 3041.
Thermostable alkaline phosphatase from Thermus sp. 3041 has been expressed in Escherichia coli, purified and crystallized. The crystals belong to space group P2(1)22(1), with unit-cell parameters a = 57.7, b = 69.9, c = 111.5 A. Diffraction data were collected to 2.54 A with a completeness of 91.1% (87.8% for the last shell), an R(merge) value of 0.105 (0.312) and an I/sigma(I) value of 9.5 (3.6).
Institute of Genetics, School of Life Science, Fudan University, Shanghai, People's Republic of China.
C N
CN
Ji
T
T
Jiang
M Q
MQ
Chen
X Y
XY
Sheng
Y M
YM
Mao
D000469:Alkaline Phosphatase / Q000737:chemistry* / Q000302:isolation & purification*; D003460:Crystallization; D004795:Enzyme Stability; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D013329:Structure-Activity Relationship; D013696:Temperature; D013824:Thermus / Q000201:enzymology*; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D000469:Alkaline Phosphatase