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- W2887998529 abstract "Cryo-electron microscopy (cryo-EM) has become a major technique for protein structure determination. Many atomic structures have been derived from cryo-EM density maps of about 3Å resolution. Side-chain conformations are well determined in density maps with super-resolutions such as 1-2Å. It is desirable to have a statistical method to detect anomalous side-chains without a super-resolution density map. In this study, we analyzed structures derived from X-ray density maps with higher than 1.5Å resolution and those from cryo-EM density maps with 2-4 Å and 4-6 Å resolutions respectively. We introduce a histogram-based outlier score (HBOS) for anomaly detection in protein models built from cryo-EM density maps. This method uses the statistics derived from X-ray dataset (<1.5Å) as the reference and combines five features involving the distal block distance, side-chain length, phi, psi, and first chi angle of the residue. Higher percentages of anomalies were observed in the cryo-EM models than in the super-resolution X-ray models. Lower percentages of anomalies were observed in cryo-EM models derived after January 2017 than those derived before 2017." @default.
- W2887998529 created "2018-08-31" @default.
- W2887998529 creator A5049641499 @default.
- W2887998529 creator A5078143614 @default.
- W2887998529 date "2018-08-15" @default.
- W2887998529 modified "2023-10-17" @default.
- W2887998529 title "Using Combined Features to Analyze Atomic Structures derived from Cryo-EM Density Maps" @default.
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- W2887998529 doi "https://doi.org/10.1145/3233547.3233709" @default.
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