| Title : Crystallization and preliminary X-ray diffraction studies of the carboxylesterase EST2 from Alicyclobacillus acidocaldarius - De Simone_1999_Acta.Crystallogr.D.Biol.Crystallogr_55_1348 |
| Author(s) : De Simone G , Manco G , Galdiero S , Lombardi A , Rossi M , Pavone V |
| Ref : Acta Crystallographica D Biol Crystallogr , 55 :1348 , 1999 |
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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. |
| PubMedSearch : De Simone_1999_Acta.Crystallogr.D.Biol.Crystallogr_55_1348 |
| PubMedID: 10393304 |
| Gene_locus related to this paper: aliac-est2 |
| Gene_locus | aliac-est2 |
De Simone G, Manco G, Galdiero S, Lombardi A, Rossi M, Pavone V (1999)
Crystallization and preliminary X-ray diffraction studies of the carboxylesterase EST2 from Alicyclobacillus acidocaldarius
Acta Crystallographica D Biol Crystallogr
55 :1348
De Simone G, Manco G, Galdiero S, Lombardi A, Rossi M, Pavone V (1999)
Acta Crystallographica D Biol Crystallogr
55 :1348