Macromolecular complexes in crystals and solutions.
Macromolecular complexes in crystals and solutions.
复制标题
DOI：
10.1107/s0907444911007232
复制
发表时间：
2011-04
期刊：
影响因子：
--
通讯作者：
Krissinel E
中科院分区：
文献类型：
--
作者：
Krissinel E
描述和讨论了分析大分子复合物和相互作用之间的关系及其在晶体堆积中的表现的方法。本文介绍了现有的方法进行分析的大分子相互作用和复杂的晶体包装的讨论。提出并讨论了在普通程序中可能得到错误答案的典型情况和条件。更普遍的问题是什么之间的关系是自然（溶剂）和结晶组件进行了讨论和研究。计算分析表明，弱相互作用与K d ≥ 100 µM在结晶过程中损失的可能性很大。 在这种情况下，晶体堆积错误地代表了大分子复合物和相互作用。对于PDB中多达20%的蛋白质二聚体，错误表达的可能性估计高于50%。鉴于弱大分子相互作用在许多生化过程中发挥了重要作用，这些结果表明，一个互补的非晶体学研究时，应始终进行推断弱结合复合物的结构方面。
Methods for the analysis of the relationship between macromolecular complexes and interactions and their manifestation in crystal packing are described and discussed. This paper presents a discussion of existing methods for the analysis of macromolecular interactions and complexes in crystal packing. Typical situations and conditions where wrong answers may be obtained in the course of ordinary procedures are presented and discussed. The more general question of what the relationship is between natural (in-solvent) and crystallized assemblies is discussed and researched. A computational analysis suggests that weak interactions with K d ≥ 100 µM have a considerable chance of being lost during the course of crystallization. In such instances, crystal packing misrepresents macromolecular complexes and interactions. For as many as 20% of protein dimers in the PDB the likelihood of misrepresentation is estimated to be higher than 50%. Given that weak macromolecular interactions play an important role in many biochemical processes, these results suggest that a complementary noncrystallographic study should be always conducted when inferring structural aspects of weakly bound complexes.