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  • Title: Crystallization and preliminary X-ray diffraction analysis of Leishmania major dihydroorotate dehydrogenase.
    Author: Cordeiro AT, Feliciano PR, Nonato MC.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2006 Oct 01; 62(Pt 10):1049-51. PubMed ID: 17012810.
    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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