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-Structure paper
タイトル | Measurement of atom resolvability in cryo-EM maps with Q-scores. |
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ジャーナル・号・ページ | Nat Methods, Vol. 17, Issue 3, Page 328-334, Year 2020 |
掲載日 | 2020年2月10日 |
![]() | Grigore Pintilie / Kaiming Zhang / Zhaoming Su / Shanshan Li / Michael F Schmid / Wah Chiu / ![]() |
PubMed 要旨 | 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. |
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手法 | EM (単粒子) |
解像度 | 1.75 - 3.08 Å |
構造データ | ![]() EMDB-20026: ![]() EMDB-20027: ![]() EMDB-20028: |
由来 |
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