2020Sazzed helices

Citation

Sazzed, S.; Scheible, P.; Alshammari, M.; Wriggers, W., He, J. Cylindrical Similarity Measurement for Helices in Medium-Resolution Cryo-Electron Microscopy Density Maps. Journal of chemical information and modeling, 2020, 60, 2644-2650

Abstract

Cryo-electron microscopy (cryo-EM) density maps at medium resolution (5-10 Å) reveal secondary structural features such as α-helices and β-sheets, but they lack the side chain details that would enable a direct structure determination. Among the more than 800 entries in the Electron Microscopy Data Bank (EMDB) of medium-resolution density maps that are associated with atomic models, a wide variety of similarities can be observed between maps and models. To validate such atomic models and to classify structural features, a local similarity criterion, the score, is proposed and evaluated in this study. The score is theoretically normalized to a range from zero to one, providing a local measure of cylindrical agreement between the density and atomic model of a helix. A systematic scan of 30,994 helices (among 3,247 protein chains modeled into medium-resolution density maps) reveals an actual range of observed scores from 0.171 to 0.848, suggesting that the cylindrical fit of the current data is well stratified by the proposed measure. The best (highest) scores tend to be associated with regions that exhibit high and spatially homogeneous local resolution (between 5 Å and 7.5 Å) in the helical density. The proposed scores can be used as a discriminative classifier for validation studies and as a ranking criterion for cryo-EM density features in databases.

Links

https://pubs.acs.org/doi/10.1021/acs.jcim.0c00010