ArticleActa crystallographica. Section D, Structural biology2020
Amyloid structure determination in RELION-3.1.
Article in Acta crystallographica. Section D, Structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 183 papers.
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Who cites it
183 citing papers in PubMed.
- Polymorphic structures of rapidly twisting 40-residue amyloid-β fibrils.Biophysical journal · 2026Article
- Repositioning of polyubiquitin alters the pathologic tau filament structure.Nature structural & molecular biology · 2026Article
- An N-terminal ATTR Fibril Segment Promotes Transthyretin Amyloid Nucleation and Polymorphism.bioRxiv : the preprint server for biology · 2026Article
- Conserved catalytic motifs encode enzyme-like supramolecular peptide assemblies.Research square · 2026Article
- Core nucleosomes are refractory to lentiviral DNA integration.Nature communications · 2026Article
- Distinct amyloid-β filament fold in individuals with APP Flemish mutation.Nature structural & molecular biology · 2026Article
- WebCalEM: a browser-based tool for routine and accurate pixel-size calibration in cryo-EM.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Polymorphic IGLV6-57 AL amyloid fibrils and features of a shared folding pathway.Nature communications · 2026Article
- Supramolecular nanofiber stabilization of microdroplets enables ultra-sensitive virus infection analysis.Nature communications · 2026Article
- The amyloid packing difference: A pairwise comparison metric for amyloid structures.Structure (London, England : 1993) · 2026Article
- Helical reconstruction of amyloids in cryoSPARC.Acta crystallographica. Section F, Structural biology communications · 2026Article
- A functional amyloid scaffold shapes insect egg coats.bioRxiv : the preprint server for biology · 2026Article
- WebCalEM: a browser-based tool for routine and accurate pixel size calibration in cryo-EM.bioRxiv : the preprint server for biology · 2026Article
- Article
- Cysteines are critical determinants of spontaneous and seeded tau aggregation in cells.Research square · 2026Article
- The molecular mechanism of the cyanobacterial bicarbonate importer CmpABCD activated by the intracellular nitrate.Nature communications · 2026Article
- Cryo-EM reveals structural variability of apolipoprotein A-I amyloid fibrils across organs, mutations, and clinical presentations.Nature communications · 2026Article
- Polymorphic structures of rapidly twisting 40-residue amyloid-β fibrils.bioRxiv : the preprint server for biology · 2026Article
- Structural polymorphism of ex-vivo ALECT2 amyloid fibrils revealed by cryo-EM.Nature communications · 2026Article
- Article
123 more citing papers are in PubMed but not listed here.
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Abstract
Helical reconstruction in RELION is increasingly being used to determine the atomic structures of amyloid filaments from electron cryo-microscopy (cryo-EM) images. However, because the energy landscape of amyloid refinements is typically fraught with local optima, amyloid structure determination is often difficult. This paper aims to help RELION users in this process. It discusses aspects of helical reconstruction that are particularly relevant to amyloids, it illustrates the problem of local optima in refinement and how to detect them, and it introduces a new method to calculate 3D initial models from reference-free 2D class averages. By providing starting models that are closer to the global optimum, this method makes amyloid structure determination easier. All methods described are open-source and distributed within RELION-3.1. Their use is illustrated using a publicly available data set on tau filaments from the brain of an individual with Alzheimer's disease.
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