ArticleBiophysical journal2017
Flexible Fitting of Atomic Models into Cryo-EM Density Maps Guided by Helix Correspondences.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Refinement of AlphaFold2 models against experimental and hybrid cryo-EM density maps.QRB discovery · 2022Article
- Three-Dimensional Graph Matching to Identify Secondary Structure Correspondence of Medium-Resolution Cryo-EM Density Maps.Biomolecules · 2021Article
- EMNUSS: a deep learning framework for secondary structure annotation in cryo-EM maps.Briefings in bioinformatics · 2021Article
- EvoSeg: Automated Electron Microscopy Segmentation through Random Forests and Evolutionary Optimization.Biomimetics (Basel, Switzerland) · 2021Article
- Multi-Scale Flexible Fitting of Proteins to Cryo-EM Density Maps at Medium Resolution.Frontiers in molecular biosciences · 2021Article
- Advances in Structure Modeling Methods for Cryo-Electron Microscopy Maps.Molecules (Basel, Switzerland) · 2019Review
- Accurate flexible refinement of atomic models against medium-resolution cryo-EM maps using damped dynamics.BMC structural biology · 2018Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Although electron cryo-microscopy (cryo-EM) has recently achieved resolutions of better than 3 Å, at which point molecular modeling can be done directly from the density map, analysis and annotation of a cryo-EM density map still primarily rely on fitting atomic or homology models to the density map. In this article, we present, to our knowledge, a new method for flexible fitting of known or modeled protein structures into cryo-EM density maps. Unlike existing methods that are guided by local density gradients, our method is guided by correspondences between the α-helices in the density map and model, and does not require an initial rigid-body fitting step. Compared with current methods on both simulated and experimental density maps, our method not only achieves greater accuracy for proteins with large deformations but also runs as fast or faster than many of the other flexible fitting routines.
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Registered trials
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