Crystallization and preliminary X-ray diffraction analysis of ybfF, a new esterase from Escherichia coli K12.
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%.
Park
Suk Youl
SY
Department of Chemistry and Institute of Basic Sciences, Chonnam National University, Gwangju 500-757, Republic of Korea.
Lee
Sang Hak
SH
Lee
Jieun
J
Jung
Che Hun
CH
Kim
Jeong Sun
JS
D003460:Crystallization; D048168:Escherichia coli K12 / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D004950:Esterases / Q000737:chemistry*; D014961:X-Ray Diffraction
D029968:Escherichia coli Proteins; D004950:Esterases; C526138:ybfF protein, E coli