首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Features of the secondary structure of a protein molecule from powder diffraction data.
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Features of the secondary structure of a protein molecule from powder diffraction data.

机译:蛋白质的二级结构的特性分子从粉末衍射数据。

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Protein powder diffraction is shown to be suitable for obtaining de novo solutions to the phase problem at low resolution via phasing methods such as the isomorphous replacement method. Two heavy-atom derivatives (a gadolinium derivative and a holmium derivative) of the tetragonal form of hen egg-white lysozyme were crystallized at room temperature. Using synchrotron radiation, high-quality powder patterns were collected in which pH-induced anisotropic lattice-parameter changes were exploited in order to reduce the challenging and powder-specific problem of overlapping reflections. The phasing power of two heavy-atom derivatives in a multiple isomorphous replacement analysis enabled molecular structural information to be obtained up to approximately 5.3 A resolution. At such a resolution, features of the secondary structure of the lysozyme molecule can be accurately located using programs dedicated to that effect. In addition, the quoted resolution is sufficient to determine the correct hand of the heavy-atom substructure which leads to an electron-density map representing the protein molecule of proper chirality.
机译:蛋白质粉末衍射证明是合适的获取新创解决阶段通过分阶段方法在低分辨率的问题比如同形的替代方法。重原子衍生物(钆导数和钬正方的导数)的形式母鸡蛋清溶菌酶的结晶室温。高质量的粉末收集模式这pH-induced各向异性晶格参数改变是为了减少具有挑战性和powder-specific问题重叠的倒影。重原子衍生物在多个同形替代分析使分子结构信息获得的约5.3一项决议。溶菌酶的二级结构分子可以准确查找使用程序专用的。足以确定正确的决议手重原子子结构的线索电子密度图表示蛋白质分子的手性。

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