Use of non-crystallographic symmetry in protein structure refinement
Use of non-crystallographic symmetry in protein structure refinement
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DOI：
10.1107/s0907444995016477
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发表时间：
1996-07-01
期刊：
影响因子：
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通讯作者：
Kleywegt, GJ
中科院分区：
文献类型：
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作者：
Kleywegt, GJ
描述了几种客观评估蛋白质结构（不）相似性的方法，其中一些方法，当应用于非晶体学相关的蛋白质模型时，能够区分显着差异和“随机噪声”。这些方法中的一些已经被用于研究已经通过X射线晶体学解决的数百种蛋白质结构的样品，以研究非晶体学相关的蛋白质模型彼此不同的程度。它示出，这种差异的程度在很大程度上取决于用于确定和细化的结构和测量的一些统计数据的数据的分辨率，甚至基本上线性变化的分辨率。讨论了这些发现对用于细化具有非晶体对称性的结构（特别是在低分辨率下）的策略的影响。最后，两个例子给出了最近的结构测定从这个实验室中的存在（和就业）的非晶体对称性是至关重要的解决方案和完善的结构。
Several methods to assess the (dis)similarity of protein structures objectively are described, some of which, when applied to non-crystallographically related protein models, are able to discriminate between significant differences and 'random noise'. Some of these methods have been used to investigate a sample of several hundred protein structures which have been solved by means of X-ray crystallography in order to investigate the extent to which non-crystallographically related protein models differ from one another. It is shown that the extent of such differences is largely dependent on the resolution of the data used for the determination and refinement of the structure and, measured by some statistics, even varies essentially linearly with the resolution. The implications of these findings for the strategies used to refine structures with non-crystallographic symmetry, in particular at low resolution, are discussed. Finally, two examples are given of recent structure determinations from this laboratory in which the presence (and employment) of non-crystallographic symmetry was crucial to the solution and refinement of the structure.