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Electrostatic Potentials around the Proteins Preferably Crystallized by Ammonium Sulfate

机译：蛋白质周围的静电电位优选地通过硫酸铵结晶

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摘要

Ammonium sulfate (AS) is one of the most popular precipitants in protein crystallization. However, AS is not always effective for all kinds of proteins. Some proteins are easily crystallized by utilizing AS, while others are not. Polyethylene glycols (PEGs) is also frequently used in protein crystallization. To clarify the reason a protein has a preference for a precipitant in crystal growth, we investigated electrostatic potentials for 100 kinds of proteins that had been crystallized by high concentrations of AS. Most of the proteins have a common shape for the isosurface of their electrostatic potentials. The positive and negative areas of electrostatic potential are almost equally separated. The contact between the positive and negative areas is limited to a narrow region on the protein surface. The separation of the electrostatic potential is neat even at the contact region. In contrast, the separation between positive and negative areas is not clear for the proteins preferably crystallized by PEGs. The positive and negative areas of electrostatic potential are fragmentary, and the isosurface at the contact region is complicated. These findings suggest that not only the local interaction between AS ions and a protein molecule but also the surroundings of the protein are responsible for crystal growth.
机译：硫酸铵（AS）是蛋白质结晶中最常用的沉淀剂之一。然而，AS并不总是对所有种类的蛋白质都有效。一些蛋白质很容易利用砷结晶，而另一些则不然。聚乙二醇（PEG）也常用于蛋白质结晶。为了阐明蛋白质在晶体生长中偏好沉淀剂的原因，我们研究了100种被高浓度砷结晶的蛋白质的静电势。大多数蛋白质的静电电位等值面形状相同。静电势的正负区域几乎是相等的。正区和负区之间的接触仅限于蛋白质表面的狭窄区域。即使在接触区域，静电势的分离也很整齐。相比之下，对于最好由PEG结晶的蛋白质，正区和负区之间的分离并不清楚。静电电位的正负区是零碎的，接触区的等值面是复杂的。这些发现表明，不仅砷离子和蛋白质分子之间的局部相互作用，而且蛋白质周围的环境也对晶体生长负责。

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  • 来源
    《Crystal growth & design》 |2021年第1期|共9页
  • 作者

    Yan Guo; Liang Qu; Noritaka Nishida; Tyuji Hoshino;

  • 作者单位

    Graduate School of Pharmaceutical Sciences Chiba University;

    Graduate School of Pharmaceutical Sciences Chiba University;

    Graduate School of Pharmaceutical Sciences Chiba University;

    Graduate School of Pharmaceutical Sciences Chiba University;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 晶体学;
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