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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Effects of macromolecular impurities and of crystallization method on the quality of eubacterial aspartyl-tRNA synthetase crystals.
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Effects of macromolecular impurities and of crystallization method on the quality of eubacterial aspartyl-tRNA synthetase crystals.

机译：高分子杂质的影响结晶质量的方法eubacterial aspartyl-tRNA合成酶晶体。

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摘要

Although macromolecular purity is thought to be essential for the growth of flawless protein crystals, only a few studies have investigated how contaminants alter the crystallization process and crystal quality. Likewise, the outcome of a crystallization process may vary with the crystallization method. Here, it is reported how these two variables affect the crystallogenesis of aspartyl-tRNA synthetase from the eubacterium Thermus thermophilus. This homodimeric enzyme (M(r) = 130 000) possesses a multi-domain architecture and crystallizes either in a monoclinic or an orthorhombic habit. Minute amounts of protein impurities alter to a different extent the growth of each crystal form. The best synthetase crystals are only obtained when the crystallizing solution is either enclosed in capillaries or immobilized in agarose gel. In these two environments convection is reduced with regard to that existing in an unconstrained solution.
机译：尽管大分子被认为是纯洁完美的蛋白质的生长所必需的晶体,只有少数的研究调查污染物如何改变结晶吗过程和晶体质量。结晶过程的结果可能不同结晶的方法。这两个变量如何影响的报道crystallogenesis aspartyl-tRNA合成酶的的真细菌栖热菌属酸奶。homodimeric酶(M (r) = 130 000)拥有一个多域结构和结晶在单斜或斜方晶系的习惯。大量的蛋白质杂质改变到一个每个晶体形成不同程度的增长。最好的合成酶晶体只获得当结晶的解决方案封闭毛细血管或固定在琼脂糖凝胶。对现有的减少无约束的解决方案。

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