title: Crystallization and preliminary X-ray diffraction data for the carboxylesterase Est30 from Bacillus stearothermophilus.
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.
authors.affiliation: Biology Department, Georgia State University, Atlanta, GA, USA.
authors.forename: Ping
authors.initials: P
authors.lastname: Liu
authors.forename: Yuan-Fang
authors.initials: YF
authors.lastname: Wang
authors.forename: Hosam E
authors.initials: HE
authors.lastname: Ewis
authors.forename: Ahmed
authors.initials: A
authors.lastname: Abdelal
authors.forename: Chung Dar
authors.initials: CD
authors.lastname: Lu
authors.forename: Irene T
authors.initials: IT
authors.lastname: Weber
mesh_terms: 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
chemical_list: D011994:Recombinant Proteins; D043182:Carboxylesterase; C483833:carboxylesterase Est30, Bacillus; D000645:Ammonium Sulfate