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 Ê resolution, using a single frozen crystal.
Crystallization and preliminary X-ray diffraction studies of the carboxylesterase EST2 from Alicyclobacillus acidocaldarius / G., DE SIMONE; G., Manco; Galdiero, Stefania; Lombardi, Angelina; M., Rossi; Pavone, Vincenzo. - In: ACTA CRYSTALLOGRAPHICA. SECTION D, BIOLOGICAL CRYSTALLOGRAPHY. - ISSN 0907-4449. - STAMPA. - 55:(1999), pp. 1348-1349.
Crystallization and preliminary X-ray diffraction studies of the carboxylesterase EST2 from Alicyclobacillus acidocaldarius
GALDIERO, STEFANIA;LOMBARDI, ANGELINA;PAVONE, VINCENZO
1999
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 Ê resolution, using a single frozen crystal.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
