ArticleMethods in molecular biology (Clifton, N.J.)2025
High-Resolution Cryo-EM Analyses of Nucleosomes.
Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Cryo-EM structures of CENP-A nucleosomes isolated from human cells.Communications biology · 2026Article
- A method for cryo-EM analysis of eukaryotic nucleosomes reconstituted in bacterial cells.iScience · 2026Article
- Preparation of Chromatin Fragments From Human Cells for Cryo-EM Analysis.Bio-protocol · 2025Article
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Authors and funding
5 authors.
Funding
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Abstract
The fundamental chromatin unit is the nucleosome, in which approximately 150 base pairs of DNA are bound to the surface of a symmetric histone octamer containing 2 copies each of histones H2A, H2B, H3, and H4. Over the years, numerous structures of nucleosomes have been determined by X-ray crystallography. However, their structural and functional versatility may not have been fully revealed, due to crystal packing effects. Various structures of nucleosomes and their complexes with nucleosome-binding proteins are now being determined by cryo-electron microscopy (cryo-EM) single-particle analysis, allowing the visualization of their structural diversity. In this report, we present a method for high-resolution structural analyses of nucleosomes by cryo-EM and describe the detailed procedures for nucleosome purification, cryo-EM grid preparation, data collection, and data processing. This method can serve as a good starting point for cryo-EM investigations of nucleosomes and their wide range of complexes.
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