As more atomic structures are determined from cryo-electron microscopy (cryo-EM) density maps, validation of such structures is an important task. We report findings after analyzing the change of cryo-EM structures in a comparison between those released by December 2016 and those released between 2017 and 2019. The cryo-EM models created from density maps with resolution better than 6 Å were divided into six data sets. A histogram-based outlier score (HBOS) was implemented and validation reports were collected from the Protein Data Bank. The results suggest that the overall quality of EM structures released after December 2016 is better than that of structures released before 2017. The conformation qualities of most residue types might have been improved, except for Leucine, Phenylalanine, and Serine in high-resolution datasets (higher than 4 Å). We observe that structures solved from 0-4 Å resolution density maps have an almost identical HBOS profile as that of structures derived from density maps with 4-6 Å resolution.
Keywords: X-ray; anomaly; cryo-electron microscopy; machine learning; protein structure; side-chain; statistics; validation.