title: Crystallization and preliminary crystallographic analysis of formyl-CoA tranferase from Oxalobacter formigenes.
abstract: 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 A 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 A. 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.
authors.affiliation: Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden.
authors.forename: Stefano
authors.initials: S
authors.lastname: Ricagno
authors.forename: Stefan
authors.initials: S
authors.lastname: Jonsson
authors.forename: Nigel
authors.initials: N
authors.lastname: Richards
authors.forename: Ylva
authors.initials: Y
authors.lastname: Lindqvist
mesh_terms: D001051:Apoenzymes / Q000737:chemistry; D003065:Coenzyme A / Q000737:chemistry; D015256:Coenzyme A-Transferases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D020624:Oxalobacter formigenes / Q000201:enzymology*; D011092:Polyethylene Glycols; D011994:Recombinant Proteins
chemical_list: D001051:Apoenzymes; D011994:Recombinant Proteins; D011092:Polyethylene Glycols; D015256:Coenzyme A-Transferases; C064813:formyl-coenzyme A transferase; D003065:Coenzyme A