Crystallization of native and selenomethionyl yeast orotidine 5'-phosphate decarboxylase.
Crystals of the Saccharomyces cerevisiae pyrimidine biosynthetic enzyme orotidine 5'-phosphate decarboxylase (ODCase) were grown by the hanging-drop vapor-diffusion technique at 277 K using polyethylene glycol 4000 as the precipitant. Crystals of native and selenomethionyl ODCase diffract to less than 2.2 A and belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 90.1, b = 116.2, c = 117.0 A. Crystals of ODCase grown in the presence of the postulated transition-state analog inhibitor 6-hydroxyuridine 5'--phosphate (BMP) diffract to less than 2.5 A and belong to space group P2(1), with unit-cell parameters a = 79.9, b = 80.0, c = 98.2 A, beta = 108.6 degrees.
Miller
B G
BG
Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599-7260, USA.
Hassell
A M
AM
Milburn
M V
MV
Short
S A
SA
D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D009964:Orotidine-5'-Phosphate Decarboxylase / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D012645:Selenomethionine / Q000378:metabolism
D011994:Recombinant Proteins; D012645:Selenomethionine; D009964:Orotidine-5'-Phosphate Decarboxylase