ArticleProceedings of the National Academy of Sciences of the United States of America2020
Cryogenic single-molecule fluorescence annotations for electron tomography reveal in situ organization of key proteins in
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 111 citations in OpenAlex.
- Super-resolution atlas of SARS-CoV-2 infection reveals protease-dependent organelle maturation, dsRNA landscapes, and intracellular structural proteins.Nature communications · 2026Article
- A tunable aqueous architecture modulates functional output in biomolecular condensates.bioRxiv : the preprint server for biology · 2026Article
- Cryogenic electron tomography by the numbers: Charting underexplored lineages in structural cell biology.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Fully genetically encoded low-molecular-weight protein tags with defined shapes for direct molecular identification by cryo-electron tomography.bioRxiv : the preprint server for biology · 2026Article
- Optical interference for the guidance of cryogenic focused ion beam milling beyond the axial diffraction limit.Nature communications · 2026Article
- Visualizing Postsynaptic Density in Excitatory Synapses with Electron Tomography.Advances in neurobiology · 2026Review
- Cryogenic light microscopy of vitrified samples with angstrom precision.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cryoprotectants-assisted plunge freezing of thick brain tissue specimens for targeted physiologically relevant cryo-imagingbioRxiv : the preprint server for biology · 2025Article
- Time-deterministic cryo-optical microscopy.Light, science & applications · 2025Article
- Cryo-light microscopy with angstrom precision deciphers structural conformations of PIEZO1 in its native state.Science advances · 2025Article
- Super-resolution microscopy for structural biology.Nature methods · 2025Review
- High-throughput cryo-electron tomography enables multiscale visualization of the inner life of microbes.Current opinion in structural biology · 2025Review
- Multivalency Controls the Growth and Dynamics of a Biomolecular Condensate.Journal of the American Chemical Society · 2025Article
- Quantitative spatial analysis of chromatin biomolecular condensates using cryoelectron tomography.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cryogenic single-molecule fluorescence imaging.BMB reports · 2025Review
- Quantitative Spatial Analysis of Chromatin Biomolecular Condensates using Cryo-Electron Tomography.bioRxiv : the preprint server for biology · 2024Article
- Recent advances in correlative cryo-light and electron microscopy.Current opinion in structural biology · 2024Review
- Exploring Transient States of PAmKate to Enable Improved Cryogenic Single-Molecule Imaging.Journal of the American Chemical Society · 2024Article
- Article
- Exploring transient states of PAmKate to enable improved cryogenic single-molecule imaging.bioRxiv : the preprint server for biology · 2024Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Superresolution fluorescence microscopy and cryogenic electron tomography (CET) are powerful imaging methods for exploring the subcellular organization of biomolecules. Superresolution fluorescence microscopy based on covalent labeling highlights specific proteins and has sufficient sensitivity to observe single fluorescent molecules, but the reconstructions lack detailed cellular context. CET has molecular-scale resolution but lacks specific and nonperturbative intracellular labeling techniques. Here, we describe an imaging scheme that correlates cryogenic single-molecule fluorescence localizations with CET reconstructions. Our approach achieves single-molecule localizations with an average lateral precision of 9 nm, and a relative registration error between the set of localizations and CET reconstruction of ∼30 nm. We illustrate the workflow by annotating the positions of three proteins in the bacterium
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.