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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Rapid model building of alpha-helices in electron-density maps.
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Rapid model building of alpha-helices in electron-density maps.

机译：快速的阿尔法螺旋模型建立电子密度图。

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摘要

A method for the identification of alpha-helices in electron-density maps at low resolution followed by interpretation at moderate to high resolution is presented. Rapid identification is achieved at low resolution, where alpha-helices appear as tubes of density. The positioning and direction of the alpha-helices is obtained at moderate to high resolution, where the positions of side chains can be seen. The method was tested on a set of 42 experimental electron-density maps at resolutions ranging from 1.5 to 3.8 A. An average of 63% of the alpha-helical residues in these proteins were built and an average of 76% of the residues built matched helical residues in the refined models of the proteins. The overall average r.m.s.d. between main-chain atoms in the modeled alpha-helices and the nearest atom with the same name in the refined models of the proteins was 1.3 A.
机译：阿尔法螺旋的方法识别在低分辨率电子密度图其次是解释在中度到高决议。实现在低分辨率,阿尔法螺旋表现为管的密度。阿尔法螺旋的方向了中度到高分辨率,职位可以看到的侧链。在一组42实验电子密度地图在决议从1.5到3.8不等。α螺旋残留的63%的平均水平这些蛋白质建成,平均76%残留的匹配螺旋残留改进模型的蛋白质。平均r.m.s.d.主链原子之间建模阿尔法螺旋和最近的原子改进模型的相同的名称蛋白质是1.3。

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