Finzel B C, Salemme F R
Nature. 1985;315(6021):686-8. doi: 10.1038/315686a0.
Atomic temperature factors (B-values) obtained from X-ray refinement experiments provide empirical estimates of protein mobility that have been correlated with both theoretical simulations of protein dynamics and experimental studies of antibody reactivity. The comparison of B-values with protein solution properties requires adjustment of the apparent atomic mobilities to compensate for the effects of the crystal environment. Here we compare crystallographically independent subunits of the dimeric cytochrome c' from the bacterium Rhodospirillum molischianum to examine how lattice effects influence refined B-values. In addition to local effects on protein mobility at crystal contacts, we show that B-value differences up to 12 A between subunits result from lattice disordering effects that approximate to concerted rotations of the molecules about a crystal symmetry axis.
通过X射线精修实验获得的原子温度因子（B值）提供了蛋白质流动性的经验估计值，这些估计值已与蛋白质动力学的理论模拟以及抗体反应性的实验研究相关联。将B值与蛋白质溶液性质进行比较时，需要调整表观原子迁移率，以补偿晶体环境的影响。在此，我们比较了来自球形红假单胞菌的二聚体细胞色素c'的晶体学独立亚基，以研究晶格效应如何影响精修后的B值。除了对晶体接触处蛋白质流动性的局部影响外，我们还表明，亚基之间高达12 Å的B值差异是由晶格无序效应导致的，这种效应近似于分子围绕晶体对称轴的协同旋转。
