Crystallization and preliminary X-ray diffraction studies of the carboxylesterase EST2 from Alicyclobacillus acidocaldarius

G De Simone; G Manco; S Galdiero; A Lombardi; M Rossi; V Pavone

doi:10.1107/s0907444999005156

Crystallization and preliminary X-ray diffraction studies of the carboxylesterase EST2 from Alicyclobacillus acidocaldarius

Acta Crystallogr D Biol Crystallogr. 1999 Jul;55(Pt 7):1348-9. doi: 10.1107/s0907444999005156.

Authors

G De Simone¹, G Manco, S Galdiero, A Lombardi, M Rossi, V Pavone

Affiliation

¹ 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.

PMID: 10393304
DOI: 10.1107/s0907444999005156

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacillaceae / enzymology*
Carboxylic Ester Hydrolases / chemistry*
Crystallization
Crystallography, X-Ray
Protein Conformation

Substances

Carboxylic Ester Hydrolases