Electronic Reprint Biological Crystallography Optimal Description of a Protein Structure in Terms of Multiple Groups Undergoing Tls Motion Biological Crystallography Optimal Description of a Protein Structure in Terms of Multiple Groups Undergoing Tls Mot
Electronic Reprint Biological Crystallography Optimal Description of a Protein Structure in Terms of Multiple Groups Undergoing Tls Motion Biological Crystallography Optimal Description of a Protein Structure in Terms of Multiple Groups Undergoing Tls Mot
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发表时间：
2005
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通讯作者：
J. Painter;E. Merritt
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作者：
J. Painter;E. Merritt
本文的作者可以在自己的网站上加载此重印本，前提是保留此封面。未经IUCr事先书面许可，不得转载本文或将其存储在电子数据库等中。单个蛋白质晶体结构包含有关蛋白质动态特性的信息，并提供一个三维构象的静态视图。这些额外的信息可以在观察到的每个原子平均位置的电子密度分布中找到。一般的做法是通过为每个原子中心细化单独的原子位移参数（ADP）来解释这一点。然而，这些相同的位移往往被描述为更简单的模型的基础上TLS（平移/天平动/螺旋）刚体运动的大集团的原子，例如域间铰链运动。一个程序，TLSMD，已经开发，分析ADP的分布在以前精制的蛋白质晶体结构，以产生最佳的多组TLS描述的组成蛋白质链。TLSMD适用于任何分辨率的晶体结构。通过TLSMD分析生成的模型可以显着改善标准晶体学残差R和R free，并可以揭示蛋白质的内在动力学性质。
Author(s) of this paper may load this reprint on their own web site provided that this cover page is retained. Republication of this article or its storage in electronic databases or the like is not permitted without prior permission in writing from the IUCr. A single protein crystal structure contains information about dynamic properties of the protein as well as providing a static view of one three-dimensional conformation. This additional information is to be found in the distribution of observed electron density about the mean position of each atom. It is general practice to account for this by refining a separate atomic displacement parameter (ADP) for each atomic center. However, these same displacements are often described well by simpler models based on TLS (translation/ libration/screw) rigid-body motion of large groups of atoms, for example interdomain hinge motion. A procedure, TLSMD, has been developed that analyzes the distribution of ADPs in a previously refined protein crystal structure in order to generate optimal multi-group TLS descriptions of the constituent protein chains. TLSMD is applicable to crystal structures at any resolution. The models generated by TLSMD analysis can significantly improve the standard crystallographic residuals R and R free and can reveal intrinsic dynamic properties of the protein.