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 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.
Ricagno
Stefano
S
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden.
Jonsson
Stefan
S
Richards
Nigel
N
Lindqvist
Ylva
Y
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
D001051:Apoenzymes; D011994:Recombinant Proteins; D011092:Polyethylene Glycols; D015256:Coenzyme A-Transferases; C064813:formyl-coenzyme A transferase; D003065:Coenzyme A