ArticleNature communications2023
A minority of final stacks yields superior amplitude in single-particle cryo-EM.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Cryo-EM structure of human NaNature communications · 2026Article
- Equivalent gain-of-function variants in KCNK3 and KCNK9 and their contribution to distinct TASK K2P channelopathies.The Journal of general physiology · 2026Article
- High-resolution structures of human NHE6 and NHE9 elucidate endosomal ion and lipid interactions.Nature communications · 2026Article
- Structural Characterization of Native RNA Polymerase II Transcription Complexes and Nucleosomes in Drosophila melanogaster.Nature communications · 2026Article
- Supramolecular nanofiber stabilization of microdroplets enables ultra-sensitive virus infection analysis.Nature communications · 2026Article
- Structural basis of the regulation by CDK11 kinase of early spliceosome activation and evidence for its proofreading by DHX15 helicase.Nature communications · 2026Article
- Egyptian rousette bat humoral immunity to H9 influenza hemagglutinin.bioRxiv : the preprint server for biology · 2026Article
- Structural insights into subtype-specific agonist recognition by sphingosine-1-phosphate receptors.PLoS biology · 2026Article
- Absolute hand determination of glycofibrils from natural sources in cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Psychedelics elicit their effects by 5-HTNature · 2026Article
- Structures of the human glucose-6-phosphate transporter provide insights into its transport cycle and substrate recognition.PLoS biology · 2026Article
- Fine-tuning AlphaFold with limited cryo-EM observations.Communications chemistry · 2026Article
- Comparing cryo-EM methods and molecular dynamics simulation to investigate heterogeneity in ligand-bound TRPV1.Nature communications · 2025Article
- Capturing the native structure of membrane proteins using vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- KIDINS220 and InsP8 safeguard the stepwise regulation of phosphate exporter XPR1.Molecular cell · 2025Article
- CryoDRGN-AI: neural ab initio reconstruction of challenging cryo-EM and cryo-ET datasets.Nature methods · 2025Article
- Article
- Amortized template matching of molecular conformations from cryoelectron microscopy images using simulation-based inference.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Reducing the effects of radiation damage in cryo-EM using liquid helium temperatures.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular mechanism of PP2A/B55α phosphatase inhibition by IER5.Cell chemical biology · 2025Article
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6 authors.
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Abstract
Cryogenic electron microscopy (cryo-EM) is widely used to determine near-atomic resolution structures of biological macromolecules. Due to the low signal-to-noise ratio, cryo-EM relies on averaging many images. However, a crucial question in the field of cryo-EM remains unanswered: how close can we get to the minimum number of particles required to reach a specific resolution in practice? The absence of an answer to this question has impeded progress in understanding sample behavior and the performance of sample preparation methods. To address this issue, we develop an iterative particle sorting and/or sieving method called CryoSieve. Extensive experiments demonstrate that CryoSieve outperforms other cryo-EM particle sorting algorithms, revealing that most particles are unnecessary in final stacks. The minority of particles remaining in the final stacks yield superior high-resolution amplitude in reconstructed density maps. For some datasets, the size of the finest subset approaches the theoretical limit.
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