Crystallization and preliminary X-ray crystallographic analysis of thioesterase I from Escherichia coli

The Escherichia coli thioesterase I specifically catalyzes the deacylation of fatty acyl-CoA thioesters, especially those with long acyl groups (C-12- C-18). Single crystals of thioesterase I (E.C. 3.1.2.2) from E. coli have b een obtained using methoxypolyethylene glycol 5000 (PEG-MME 5K) as a precip itant at room temperature in 21 d. The crystals belong to the tetragonal sp ace group P4(1)2(1)2 or its enantiomorph P4(3)2(1)2, with unit-cell paramet ers a = b = 50.85 (7), c = 171.5 (1) Angstrom. The crystals diffract to bey ond 2.4 Angstrom resolution. There is one molecule of molecular weight 20.5 kDa in the asymmetric unit, with a solvent content of 55%.