Crystallization and preliminary X-ray diffraction studies of the carboxylesterase EST2 from Alicyclobacillus acidocaldarius.
EST2, a thermophilic carboxylesterase from Alicyclobacillus acidocaldarius, belonging to the HSL group of the esterase/lipase superfamily, has been crystallized for the first time. Ammonium sulfate was used as a precipitant and the crystallization proceeded at pH 7.8. The crystals belong to space group P41212 or its enantiomorph P43212, with unit-cell parameters a = b = 78.8, c = 106. 4 A. A complete data set has been collected at the synchrotron source Elettra in Trieste to 2.4 A resolution, using a single frozen crystal.
Centro Interuniversitario di Ricerca su Peptidi Bioattivi and Centro di Studio di Biocristallografia (CNR), University of Naples 'Federico II', via Mezzocannone 4, 80134 Naples, Italy.
G
G
De Simone
G
G
Manco
S
S
Galdiero
A
A
Lombardi
M
M
Rossi
V
V
Pavone
D001406:Bacillaceae / Q000201:enzymology*; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation
D002265:Carboxylic Ester Hydrolases