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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >On the molecular-replacement problem in the presence of merohedral twinning: structure of the N-terminal half-molecule of human lactoferrin.
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On the molecular-replacement problem in the presence of merohedral twinning: structure of the N-terminal half-molecule of human lactoferrin.

机译：molecular-replacement问题存在缺面的孪生:结构人类乳铁蛋白的氨基端half-molecule。

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摘要

The structure of a hemihedrally twinned protein crystal with two molecules in the asymmetric unit was solved by molecular replacement. The protein, a site-specific mutant of the N-terminal half-molecule of human lactoferrin, is able to undergo an internal rigid-body domain motion. Therefore, determining the structure required the independent positioning of four protein domains. The molecular-replacement solutions were obtained using a conventional real-space rotation function, and a translation function based on the linear correlation coefficient. Once the molecules were positioned, it was necessary to assign them to the appropriate twin domain. Several methods for doing this are described, one of which leads to a determination of the volume of each twin domain. In the appendix to the paper we discuss the interpretation of the self-rotation function in the presence of merohedral twinning.
机译：蛋白质的结构半面形的成双成对的晶体的两个分子不对称单位解决了通过分子替换。一个位点突变的氨基端half-molecule人类乳铁蛋白,能够进行一个内部的刚体运动领域。因此,确定所需的结构独立的四个定位蛋白质域。molecular-replacement解决方案使用传统的真实空间旋转基于功能和翻译功能线性相关系数。分子定位,它是必要的将它们分配给适当的双域。几种方法来执行此操作,一个导致测定的体积每双域。我们讨论的解释在固有转动功能缺面的双晶。

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