Abstract
The product of the recently discovered ybfF gene, which belongs to the esterase family, does not show high sequence similarity to other esterases. To provide the molecular background to the enzymatic mechanism of the ybfF esterase, the ybfF protein from Escherichia coli K12 (Ec_ybfF) was cloned, expressed and purified. The Ec_ybfF protein was crystallized from 60% Tacsimate and 0.1 M bis-Tris propane buffer pH 7.0. Diffraction data were collected to 1.10 A resolution using synchrotron radiation. The crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 66.09, b = 90.71, c = 92.88 A. With two Ec_ybfF molecules in the asymmetric unit, the crystal volume per unit protein weight is 2.17 A(3) Da(-1), corresponding to a solvent content of 42%.