Refined structure of orthorhombic lysozyme crystallized at high temperature: correlation between morphology and intermolecular contacts.
Refined structure of orthorhombic lysozyme crystallized at high temperature: correlation between morphology and intermolecular contacts.
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高温结晶的斜方溶菌酶的精细结构：形态与分子间接触之间的相关性。
DOI：
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发表时间：
1999
期刊：
影响因子：
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通讯作者：
Alexander A. Chernovc
中科院分区：
文献类型：
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作者：
H. Oki;Yoshiki;Matsuura;Hiroshi Komatsub;Alexander A. Chernovc
以1.7 A的分辨率对310 K结晶的正交蛋清溶菌酶（HEWL）的结构进行了细化。与主链原子的小位移相比，侧链原子相对于四方结构的大位移在许多地方被观察到。氯离子结合位点在两个分子的界面上被观察到，但在不同的位置上的结合位点在四方形式。分子间接触分析表明，存在三个独立的分子间接触，称为大键A， B和c。精氨酸侧链经常参与这些大键，这表明该残基在HEWL中的高频率可能是导致该蛋白多重多态性的原因。晶体形式是用四圆衍射仪上的光反射装置确定的。利用氢键和范德华原子相互作用的近似强度，用不同晶体平面上的组分来解释晶体形式与三维宏键网络之间的相关性。
The structure of orthorhombic hen egg-white lysozyme (HEWL) crystallized at 310 K has been refined at 1.7 A resolution. Large displacements of the side-chain atoms with respect to the tetragonal structure were observed in many places, in contrast to small displacements of the main-chain atoms. A chloride-ion binding site was observed at an interface of two molecules, but at a different position to the binding site in the tetragonal form. The analysis of intermolecular contacts in the crystal has shown the presence of three independent intermolecular contacts which are called macrobonds A, B and C. Arginine side chains are frequently involved in these macrobonds, suggesting that the high frequency of this residue in HEWL may be a possible reason for the multiple polymorphs of this protein. The crystal forms were determined using a light-reflecting device on a four-circle diffractometer. Correlations between crystal forms and the three-dimensional macrobond networks were interpreted in terms of their components in various crystallographic planes, making use of approximate strengths of hydrogen-bond and van der Waals interatomic forces.