Crystallization and preliminary X-ray diffraction studies of Aes acetyl-esterase from Escherichia coli(489 views) Sorrentino N, De Simone G, Menchise V, Mandrich L, Rossi M, Manco G, Pedone C
Keywords: Acetylesterase, Aes Protein, E Coli, Escherichia Coli Protein, Recombinant Protein, Article, Biosynthesis, Chemistry, Crystallization, Enzymology, Genetics, Metabolism, Methodology, Protein Conformation, Synchrotron, X Ray Crystallography, X-Ray, Bacteria (microorganisms),
Affiliations: *** IBB - CNR ***
Ist. Biostrutture e Bioimmagini-CNR, University of Naples 'Federico II', Via Mezzocannone 6/8, 80134 Naples, Italy
Ist. di Biochimica delle Proteine, CNR, Via P. Castellino 111, 80131 Naples, Italy
References: Not available.
Crystallization and preliminary X-ray diffraction studies of Aes acetyl-esterase from Escherichia coli
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 Angstrom. A complete data set has been collected to 2.5 Angstrom 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%.
Crystallization and preliminary X-ray diffraction studies of Aes acetyl-esterase from Escherichia coli