Crystallization and preliminary crystallographic analysis of formyl-CoA tranferase from Oxalobacter formigenes

Formyl-CoA transferase from Oxalobacter formigenes has been expressed as a recombinant protein in Escherichia coli and purified to homogeneity. Crystals of formyl-CoA transferase were grown at 293 K using polyethylene glycol 4000 as a precipitant. The diffraction pattern of flash-frozen crystals at 100 K extends to 2.2 Angstrom resolution with synchrotron radiation (lambda=0.933 nm). The crystals are tetragonal and belong to space group I4, with unit-cell parameters a=b=151.44, c=99.49 Angstrom. The asymmetric unit contains one dimer and the solvent content is 53%. Formyl-CoA transferase was crystallized both as the apoenzyme and as its complex with coenzyme A.