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| Title | Measurement of atom resolvability in cryo-EM maps with Q-scores. |
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| Journal, issue, pages | Nat Methods, Vol. 17, Issue 3, Page 328-334, Year 2020 |
| Publish date | Feb 10, 2020 |
 Authors | Grigore Pintilie / Kaiming Zhang / Zhaoming Su / Shanshan Li / Michael F Schmid / Wah Chiu /  |
| PubMed Abstract | Cryogenic electron microscopy (cryo-EM) maps are now at the point where resolvability of individual atoms can be achieved. However, resolvability is not necessarily uniform throughout the map. We ...Cryogenic electron microscopy (cryo-EM) maps are now at the point where resolvability of individual atoms can be achieved. However, resolvability is not necessarily uniform throughout the map. We introduce a quantitative parameter to characterize the resolvability of individual atoms in cryo-EM maps, the map Q-score. Q-scores can be calculated for atoms in proteins, nucleic acids, water, ligands and other solvent atoms, using models fitted to or derived from cryo-EM maps. Q-scores can also be averaged to represent larger features such as entire residues and nucleotides. Averaged over entire models, Q-scores correlate very well with the estimated resolution of cryo-EM maps for both protein and RNA. Assuming the models they are calculated from are well fitted to the map, Q-scores can be used as a measure of resolvability in cryo-EM maps at various scales, from entire macromolecules down to individual atoms. Q-score analysis of multiple cryo-EM maps of the same proteins derived from different laboratories confirms the reproducibility of structural features from side chains down to water and ion atoms. |
 External links | Nat Methods / PubMed:32042190 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 1.75 - 3.08 Å |
| Structure data |  EMDB-20026:  EMDB-20027:  EMDB-20028: |
| Source |
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Homo sapiens (human)