PMID:14501134
| Citation |
Sorrentino, N, De Simone, G, Menchise, V, Mandrich, L, Rossi, M, Manco, G and Pedone, C (2003) Crystallization and preliminary X-ray diffraction studies of Aes acetyl-esterase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 59:1846-8 |
|---|---|
| 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%. |
| Links | |
| Keywords |
Acetylesterase/biosynthesis; Acetylesterase/chemistry; Acetylesterase/genetics; Crystallization/methods; Crystallography, X-Ray/methods; Escherichia coli/enzymology; Escherichia coli Proteins; Protein Conformation; Proteins/chemistry; Proteins/metabolism; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Synchrotrons |
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