Purification, crystallization and preliminary X-ray study of orotidine 5'-monophosphate decarboxylase.
Orotidine-5'-monophosphate decarboxylase (ODCase) from Methanobacterium thermoautotrophicum has been crystallized with and without the inhibitor 6-azaUMP by the vapour-diffusion method. In the absence of the inhibitor, the protein crystallizes in space group P4(1)2(1)2 (unit-cell parameters a = b = 56.9, c = 124.5 A) with one molecule per asymmetric unit; the crystals diffract to 1.8 A resolution. In the presence of the inhibitor, the protein crystals are monoclinic, space group P2(1) (unit-cell parameters a = 73.0, b = 98.6, c = 73.3 A, gamma = 104.0 degrees ), with four molecules in the asymmetric unit; the crystals diffract to 1.5 A resolution.
Wu
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N
Department of Biochemistry, University of Toronto, 1 King's College Circle, Toronto, Ontario, M5S 1A8, Canada.
Christendat
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D
Dharamsi
A
A
Pai
E F
EF
D001483:Base Sequence; D018360:Crystallography, X-Ray; D017931:DNA Primers; D017014:Methanobacterium / Q000201:enzymology; D009964:Orotidine-5'-Phosphate Decarboxylase / Q000737:chemistry* / Q000302:isolation & purification*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D017931:DNA Primers; D011994:Recombinant Proteins; D009964:Orotidine-5'-Phosphate Decarboxylase