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Crystallization and preliminary X-ray diffraction data for the carboxylesterase Est30 from Bacillus stearothermophilus.

Ping Liu·Yuan-Fang Wang·Hosam E Ewis·Ahmed Abdelal·Chung Dar Lu·Irene T Weber
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Abstract

Crystals have been grown of the carboxylesterase Est30 from Bacillus stearothermophilus by hanging-drop vapor diffusion using ammonium sulfate as precipitant. The crystals diffracted to better than 2.0 A resolution. X-ray diffraction data were reduced in space group C222(1), with unit-cell parameters a = 55.83, b = 58.15, c = 179.65 A. R(merge) was 0.038 for 17 449 independent reflections with a completeness of 85.1%. V(M) was calculated to be 2.43 A(3) Da(-1), which suggested that there was one molecule of Est30 in the asymmetric unit. These crystals are suitable for structure determination.

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Ammonium SulfateCarboxylesteraseCrystallizationGeobacillus stearothermophilusKineticsRecombinant ProteinsTemperatureX-Ray DiffractionJournal ArticleResearch Support, U.S. Gov't, Non-P.H.S.

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Ping Liu, Yuan-Fang Wang, Hosam E Ewis, Ahmed Abdelal, Chung Dar Lu, Irene T Weber. 2003-07-23. Crystallization and preliminary X-ray diffraction data for the carboxylesterase Est30 from Bacillus stearothermophilus.. https://doi.org/10.1107/s0907444903011405

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