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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Construct optimization for studying protein complexes: obtaining diffraction-quality crystals of the pseudosymmetric PSPC1-NONO heterodimer.
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Construct optimization for studying protein complexes: obtaining diffraction-quality crystals of the pseudosymmetric PSPC1-NONO heterodimer.

机译:结构优化为研究蛋白质复合物:获得diffraction-quality晶体《pseudosymmetric PSPC1-NONO heterodimer。

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摘要

The methodology of protein crystallography provides a number of potential bottlenecks. Here, an approach to successful structure solution of a difficult heterodimeric complex of two human proteins, paraspeckle component 1 (PSPC1) and non-POU domain-containing octamer-binding protein (NONO), that are involved in gene regulation and the structural integrity of nuclear bodies termed paraspeckles is described. With the aid of bioinformatic predictions and systematic screening of a panel of constructs, bottlenecks of protein solubility, crystallization, crystal quality and crystallographic pseudosymmetry were overcome in order to produce crystals that ultimately revealed the structure.
机译:蛋白质晶体学的方法提供了许多潜在的瓶颈。一个方法成功的解决方案的结构两人的困难heterodimeric复杂1 (PSPC1)和蛋白质,paraspeckle组件non-POU domain-containing octamer-binding蛋白质(禁忌),参与基因调控和核体称为的结构完整性paraspeckles描述。生物信息学预测和系统筛选的面板结构,瓶颈蛋白质的溶解度,结晶,晶体质量和晶体伪对称克服以产生晶体最终揭示了结构。

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