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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Nonlinear temperature dependence of the crystal structure of lysozyme: correlation between coordinate shifts and thermal factors.
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Nonlinear temperature dependence of the crystal structure of lysozyme: correlation between coordinate shifts and thermal factors.

机译：非线性晶体的温度依赖性溶菌酶的结构:之间的相关性坐标转换和热的因素。

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摘要

The static and dynamic structures of human lysozyme at seven different temperatures ranging from 113 to 178 K were investigated by normal-mode refinement of the cryogenic X-ray diffraction data collected from a single crystal. Normal-mode refinement decomposes the mean-square fluctuations of protein atoms from their average position into the contributions from the internal degrees of freedom, which change the shape of the protein structure, and those from the external degrees of freedom, which generate rigid-body motions in the crystal. While at temperatures below 150 K the temperature dependence of the total mean-square fluctuations shows a small gradient similar to that predicted theoretically by normal-mode analysis, at temperatures above 150 K there is an apparent inflection in the temperature dependence with a higher gradient. The inflection in the temperature dependence at temperatures above 150 K occurs mostly in the external degrees of freedom. Possible causes for the dynamic transition are discussed with respect to the crystal packing and physicochemical properties of crystalline water.
机译：人类的静态和动态结构溶菌酶在七个不同的温度范围研究了从113年到178 K正常模式改进的低温x射线从单晶衍射数据收集。正常模式细化分解均方从他们的平均波动的蛋白质原子从内部位置的贡献自由度,这改变的形状蛋白质结构,这些从外部自由度,产生刚体运动的晶体。低于150 K的温度依赖性总均方波动显示了一个小梯度相似预测理论在正常模式分析,温度以上150 K有一个明显的拐点依赖于温度较高的梯度。的音调变化的温度依赖性温度高于150 K大多发生在外部自由度。讨论了动态过渡的尊重水晶包装和物化水晶水的性质。

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