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首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >Octamer formation in lysozyme solutions at the initial crystallization stage detected by small‐angle neutron scattering
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Octamer formation in lysozyme solutions at the initial crystallization stage detected by small‐angle neutron scattering

机译:八聚物形成的溶菌酶解决方案检测到初始结晶阶段小角中子散射

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摘要

Solutions of lysozyme in heavy water were studied by small‐angle neutron scattering (SANS) at concentrations of 40, 20 and 10?mg?ml ?1 with and without the addition of precipitant, and at temperatures of 10, 20 and 30°C. In addition to the expected protein monomers, dimeric and octameric species were identified in solutions at the maximum concentration and close to the optimal conditions for crystallization. An optimal temperature for octamer formation was identified and both deviation from this temperature and a reduction in protein concentration led to a significant decrease in the volume fractions of octamers detected. In the absence of precipitant, only monomers and a minor fraction of dimers are present in solution.
机译:解决方案重水的溶菌酶进行了研究,小角中子散射(SANS)浓度的40岁,20和10毫克?没有添加沉淀剂,温度为10、20和30°C。预期的蛋白质单体、二聚的octameric物种中标识解决方案最大浓度和接近最佳结晶条件。最佳温度为八聚物的形成识别和两个偏差温度和减少蛋白质浓度显著降低八聚物检测的体积分数。没有沉淀剂的情况下,只有单体和未成年人二聚体存在于解决方案的一部分。

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