Crystallization and preliminary X-ray diffraction data for the carboxylesterase Est30 from Bacillus stearothermophilus.
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.
Liu
Ping
P
Biology Department, Georgia State University, Atlanta, GA, USA.
Wang
Yuan-Fang
YF
Ewis
Hosam E
HE
Abdelal
Ahmed
A
Lu
Chung Dar
CD
Weber
Irene T
IT
D000645:Ammonium Sulfate / Q000737:chemistry; D043182:Carboxylesterase / Q000737:chemistry*; D003460:Crystallization; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D007700:Kinetics; D011994:Recombinant Proteins / Q000737:chemistry; D013696:Temperature; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D043182:Carboxylesterase; C483833:carboxylesterase Est30, Bacillus; D000645:Ammonium Sulfate