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  • Title: Crystallization and preliminary X-ray diffraction analysis of selenophosphate synthetases from Trypanosoma brucei and Leishmania major.
    Author: Faim LM, Rosa e Silva I, Bertacine Dias MV, D'Muniz Pereira H, Brandao-Neto J, Alves da Silva MT, Thiemann OH.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2013 Aug; 69(Pt 8):864-7. PubMed ID: 23908029.
    Abstract:
    Selenophosphate synthetase (SPS) plays an indispensable role in selenium metabolism, being responsible for catalyzing the activation of selenide with adenosine 5'-triphosphate (ATP) to generate selenophosphate, the essential selenium donor for selenocysteine synthesis. Recombinant full-length Leishmania major SPS (LmSPS2) was recalcitrant to crystallization. Therefore, a limited proteolysis technique was used and a stable N-terminal truncated construct (ΔN-LmSPS2) yielded suitable crystals. The Trypanosoma brucei SPS orthologue (TbSPS2) was crystallized by the microbatch method using paraffin oil. X-ray diffraction data were collected to resolutions of 1.9 Å for ΔN-LmSPS2 and 3.4 Å for TbSPS2.
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