Unknown

Dataset Information

0

B-factor accuracy in protein crystal structures.


ABSTRACT: The accuracy of B factors in protein crystal structures has been determined by comparing the same atoms in numerous, independent crystal structures of Gallus gallus lysozyme. Both B-factor absolute differences and normal probability plots indicate that the estimated B-factor errors are quite large, close to 9 Å2 in ambient-temperature structures and to 6 Å2 in low-temperature structures, and surprisingly are comparable to values estimated two decades ago. It is well known that B factors are not due to local movements only but reflect several, additional factors from crystal defects, large-scale disorder, diffraction data quality etc. It therefore remains essential to normalize B factors when comparing different crystal structures, although it has clearly been shown that they provide useful information about protein dynamics. Improved, quantitative analyses of raw B factors require novel experimental and computational tools that are able to disaggregate local movements from other features and properties that affect B factors.

SUBMITTER: Carugo O 

PROVIDER: S-EPMC8725162 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC4129517 | biostudies-literature
| S-EPMC2868237 | biostudies-literature
| S-EPMC6561213 | biostudies-literature
| S-EPMC5684783 | biostudies-literature
| S-EPMC2867014 | biostudies-literature
| S-EPMC3415962 | biostudies-literature
| S-EPMC126194 | biostudies-literature
| S-EPMC2775207 | biostudies-literature
| S-EPMC3546150 | biostudies-literature
| S-EPMC7749147 | biostudies-literature