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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 YisP protein from Bacillus subtilis subsp subtilis strain 168
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Crystallization and preliminary X-ray diffraction analysis of YisP protein from Bacillus subtilis subsp subtilis strain 168

机译：枯草芽孢杆菌枯草芽孢杆菌枯草芽孢杆菌菌株168的YisP蛋白的结晶和初步X射线衍射分析

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摘要

YisP is an enzyme involved in the pathway of biofilm formation in bacteria and is predicted to possess squalene synthase activity. A BlastP search using the YisP protein sequence from Bacillus subtilis subsp. subtilis strain 168 shows that it shares 23% identity with the dehydrosqualene synthase from Staphylococcus aureus. The YisP from B. subtilis 168 was expressed in Escherichia coli and the recombinant protein was purified and crystallized. The crystals, which belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 43.966, b = 77.576, c = 91.378 angstrom, were obtained by the sitting-drop vapour-diffusion method and diffracted to 1.92 angstrom resolution. Structure determination using MAD and MIR methods is in progress.
机译：YisP是一种参与细菌生物膜形成途径的酶，预计具有鲨烯合酶活性。使用来自枯草芽孢杆菌亚种的YisP蛋白序列进行BlastP搜索。枯草芽孢杆菌菌株168显示它与来自金黄色葡萄球菌的脱氢角鲨烯合酶具有23％的同一性。来自枯草芽孢杆菌168的YisP在大肠杆菌中表达，并且重组蛋白被纯化和结晶。通过坐滴蒸汽获得了属于正交晶体空间群P2（1）2（1）2（1）的晶体，晶胞参数a = 43.966，b = 77.576，c = 91.378埃。扩散法并衍射到1.92埃分辨率。使用MAD和MIR方法的结构确定正在进行中。

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