Literature DB >> 17012810

Crystallization and preliminary X-ray diffraction analysis of Leishmania major dihydroorotate dehydrogenase.

Artur T Cordeiro1, Patricia R Feliciano, M Cristina Nonato.   

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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Year:  2006        PMID: 17012810      PMCID: PMC2225193          DOI: 10.1107/S1744309106038966

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


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4.  Solvent content of protein crystals.

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Review 9.  The integration of macromolecular diffraction data.

Authors:  Andrew G W Leslie
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Review 10.  Scaling and assessment of data quality.

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Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2005-12-14
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3.  Untargeted LC-MS metabolomic studies of Asteraceae species to discover inhibitors of Leishmania major dihydroorotate dehydrogenase.

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