Ultrahigh-resolution study of protein atomic displacement parameters at cryotemperatures obtained with a helium cryostat
The contribution of temperature and other factors to the atomic displacement parameters (ADP) was estimated by comparison of models of human aldose reductase determined at 0.81 Å resolution and temperatures 15, 60 and 100 K. For ordered atoms, the differences in the isotropic equivalents of ADP were almost constant (about 1.7 Å2) while the character of the changes in ADPs was isotropic as temperature increased from 15 to 60 K. Both decreasing the data redundancy and increasing the resolution cutoff led to an increase in ADPs values.
T. Petrova, S. Ginell, A. Mitschler, I. Hazemann, T. Schneider, A. Cousido, V.Y. Lunin, A. Joachimiak and A. Podjarny
![[cryo-ADPs]](https://www.iucr.org/__data/assets/image/0011/4034/sx5054.gif)
The differences δB = B(60 K) – B(15 K) in isotropic equivalents of ADPs for CA atoms of residues in a single conformation. All values are sorted according to B values at 15 K.
