Purification, crystallization and preliminary X-ray diffraction studies on the thermostable catechol 2,3-dioxygenase of Bacillus stearothermophilus expressed in Escherichia coli.

M Q Chen; C C Yin; W Zhang; Y M Mao; Z H Zhang

doi:10.1107/s0907444997014996

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Purification, crystallization and preliminary X-ray diffraction studies on the thermostable catechol 2,3-dioxygenase of Bacillus stearothermophilus expressed in Escherichia coli.

M Q Chen·C C Yin·W Zhang·Y M Mao·Z H Zhang

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Abstract

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.

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Catechol 2,3-Dioxygenase Crystallization Dioxygenases Enzyme Stability Escherichia coli Geobacillus stearothermophilus Oxygenases Recombinant Proteins X-Ray Diffraction Journal Article Research Support, Non-U.S. Gov't

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M Q Chen, C C Yin, W Zhang, Y M Mao, Z H Zhang. 1998-05-01. Purification, crystallization and preliminary X-ray diffraction studies on the thermostable catechol 2,3-dioxygenase of Bacillus stearothermophilus expressed in Escherichia coli.. https://doi.org/10.1107/s0907444997014996

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