Crystallization and preliminary X-ray diffraction studies of the carboxylesterase EST2 from Alicyclobacillus acidocaldarius(335 views visite) De Simone G, Manco G, Galdiero S, Lombardi A, Rossi M, Pavone V
Keywords Parole chiave: Carboxylesterase, Article, Bacillaceae, Chemistry, Crystallization, Enzymology, Protein Conformation, X Ray Crystallography, Carboxylic Ester Hydrolases, X-Ray, Alicyclobacillus Acidocaldarius, Bacteria (microorganisms),
Affiliations Affiliazioni: Ctro. Interuniv. Ric. Pept. Bioatl., Centro di Stud. di Biocristallograma, University of Naples 'Federico II', via Mezzocannone 4, 80134 Naples, Italy Ist. di Biochimica delle Proteine, Enzimologia-CNR, via Marconi 10, 80125 Naples, Italy
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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 P4(1)2(1)2 or its enantiomorph P4(3)2(1)2, with unit-cell parameters a = b = 78.8, c = 106.4 Angstrom. A complete data set has been collected at the synchrotron source Elettra in Trieste to 2.4 Angstrom resolution, using a single frozen crystal.
Crystallization and preliminary X-ray diffraction studies of the carboxylesterase EST2 from Alicyclobacillus acidocaldarius
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