Title : Crystallization and preliminary X-ray diffraction studies of Aes acetyl-esterase from Escherichia coli - Sorrentino_2003_Acta.Crystallogr.D.Biol.Crystallogr_59_1846 |
Author(s) : Sorrentino N , De Simone G , Menchise V , Mandrich L , Rossi M , Manco G , Pedone C |
Ref : Acta Crystallographica D Biol Crystallogr , 59 :1846 , 2003 |
Abstract :
The acetyl-esterase Aes from Escherichia coli, which belongs to the HSL group of the esterase/lipase superfamily, has been crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 8000 as a precipitant and magnesium chloride as an additive. Crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 110.0, b = 190.6, c = 218.6 A. A complete data set has been collected to 2.5 A resolution at the Elettra synchrotron source, Trieste using a single frozen crystal. Packing density considerations agree with 10-16 monomers in the asymmetric unit, with a corresponding solvent content of 61-38%. |
PubMedSearch : Sorrentino_2003_Acta.Crystallogr.D.Biol.Crystallogr_59_1846 |
PubMedID: 14501134 |
Gene_locus related to this paper: ecoli-Aes |
Gene_locus | ecoli-Aes |
Sorrentino N, De Simone G, Menchise V, Mandrich L, Rossi M, Manco G, Pedone C (2003)
Crystallization and preliminary X-ray diffraction studies of Aes acetyl-esterase from Escherichia coli
Acta Crystallographica D Biol Crystallogr
59 :1846
Sorrentino N, De Simone G, Menchise V, Mandrich L, Rossi M, Manco G, Pedone C (2003)
Acta Crystallographica D Biol Crystallogr
59 :1846