Purification, crystallization and preliminary X-ray diffraction studies on the thermostable catechol 2,3-dioxygenase of Bacillus stearothermophilus expressed in Escherichia coli.
The thermostable catechol 2,3-dioxygenase of Bacillus stearothermophilus has been crystallized. The crystal is probably in the space group I222 with unit-cell dimensions of a = 70.87, b = 74.60 and c = 133.69 A. A native data set has been collected with a completeness of 96% at 2.22 A resolution and an Rmerge value of 0.091.
Chen
M Q
MQ
Research Group of Structural Biology and Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, China. mqchen@fudan.edu.cn
Yin
C C
CC
Zhang
W
W
Mao
Y M
YM
Zhang
Z H
ZH
D050557:Catechol 2,3-Dioxygenase; D003460:Crystallization; D049308:Dioxygenases; D004795:Enzyme Stability; D004926:Escherichia coli; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D010105:Oxygenases / Q000737:chemistry / Q000302:isolation & purification* / Q000502:physiology; D011994:Recombinant Proteins / Q000096:biosynthesis; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D010105:Oxygenases; D049308:Dioxygenases; D050557:Catechol 2,3-Dioxygenase