Crystallization and preliminary X-ray diffraction analysis of Leishmania major dihydroorotate dehydrogenase.
Artur T Cordeiro, Patricia R Feliciano, M Cristina Nonato
Index: Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62(Pt 10) , 1049-51, (2006)
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Abstract
Dihydroorotate dehydrogenases (DHODHs) are flavin-containing enzymes that catalyze the oxidation of L-dihydroorotate to orotate, the fourth step in the de novo pyrimidine nucleotide synthesis pathway. In this study, DHODH from Leishmania major has been crystallized by the vapour-diffusion technique using lithium sulfate as the precipitating agent. The crystals belong to space group P6(1), with unit-cell parameters a = 143.7, c = 69.8 A. X-ray diffraction data were collected to 2.0 A resolution using an in-house rotating-anode generator. Analysis of the solvent content and the self-rotation function indicate the presence of two molecules in the asymmetric unit. The structure has been solved by the molecular-replacement technique.
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