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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Crystallization and preliminary X-ray diffraction analysis of selenophosphate synthetases from Trypanosoma brucei and Leishmania major
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Crystallization and preliminary X-ray diffraction analysis of selenophosphate synthetases from Trypanosoma brucei and Leishmania major

机译：布氏锥虫和利什曼原虫的硒代磷酸酯合成酶的结晶和初步X射线衍射分析

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摘要

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 (Delta N-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 angstrom for Delta N-LmSPS2 and 3.4 angstrom for TbSPS2.
机译：硒磷酸合成酶（SPS）在硒代谢中起着不可或缺的作用，它负责用5'-三磷酸腺苷（ATP）催化硒化物的活化以生成硒磷酸，硒磷酸是硒代半胱氨酸合成所必需的硒供体。重组全长利什曼原虫主要SPS（LmSPS2）难以结晶。因此，使用了有限的蛋白水解技术，稳定的N末端截短的构建体（Delta N-LmSPS2）产生了合适的晶体。用石蜡油通过微分批法结晶布鲁氏锥虫SPS直系同源物（TbSPS2）。收集的X射线衍射数据的Delta N-LmSPS2分辨率为1.9埃，TbSPS2分辨率为3.4埃。

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