1. Crystallization and preliminary X-ray diffraction studies of Aes acetyl-esterase from Escherichia coli
- Author
-
Valeria Menchise, Giuseppe Manco, Giuseppina De Simone, Luigi Mandrich, Nicola Sorrentino, Carlo Pedone, and Mosè Rossi
- Subjects
Protein Conformation ,chemistry.chemical_element ,Polyethylene glycol ,Crystallography, X-Ray ,Esterase ,law.invention ,chemistry.chemical_compound ,Structural Biology ,law ,Escherichia coli ,Crystallization ,Lipase ,biology ,Magnesium ,Escherichia coli Proteins ,Resolution (electron density) ,Proteins ,General Medicine ,Recombinant Proteins ,Crystallography ,chemistry ,X-ray crystallography ,biology.protein ,Orthorhombic crystal system ,Acetylesterase ,Synchrotrons - 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%.
- Published
- 2003