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

Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1472-3. doi: 10.1107/s0907444903011405. Epub 2003 Jul 23.

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Ammonium Sulfate / chemistry
  • Carboxylesterase / chemistry*
  • Crystallization
  • Geobacillus stearothermophilus / enzymology*
  • Kinetics
  • Recombinant Proteins / chemistry
  • Temperature
  • X-Ray Diffraction

Substances

  • Recombinant Proteins
  • Carboxylesterase
  • carboxylesterase Est30, Bacillus
  • Ammonium Sulfate