ArticleJournal of computational biology : a journal of computational molecular cell biology2017
Cross-Validation of Data Compatibility Between Small Angle X-ray Scattering and Cryo-Electron Microscopy.
Article in Journal of computational biology : a journal of computational molecular cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Two datasets are better than one: method of double moments for 3D reconstruction in cryo-EM.Inverse problems · 2026Article
- Fitting high-resolution electron density maps from atomic models to solution scattering data.Biophysical journal · 2023Article
- Emerging Themes in CryoEM─Single Particle Analysis Image Processing.Chemical reviews · 2022Review
- Calculating small-angle scattering intensity functions from electron-microscopy images.RSC advances · 2022Article
- Protein Footprinting: Auxiliary Engine to Power the Structural Biology Revolution.Journal of molecular biology · 2020Review
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Authors and funding
3 authors.
Funding
Abstract
Cryo-electron microscopy (EM) and small angle X-ray scattering (SAXS) are two different data acquisition modalities often used to glean information about the structure of large biomolecular complexes in their native states. A SAXS experiment is generally considered fast and easy but unveils the structure at very low resolution, whereas a cryo-EM experiment needs more extensive preparation and postacquisition computation to yield a three-dimensional (3D) density map at higher resolution. In certain applications, we may need to verify whether the data acquired in the SAXS and cryo-EM experiments correspond to the same structure (e.g., before reconstructing the 3D density map in EM). In this article, a simple and fast method is proposed to verify the compatibility of the SAXS and EM experimental data. The method is based on averaging the two-dimensional correlation of EM images and the Abel transform of the SAXS data. Orientational preferences are known to exist in cryo-EM experiments, and we also consider these effects on our method. The results are verified on simulations of conformational states of large biomolecular complexes.
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Registered trials
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