ArticleNature communications2019
A 3.8 Å resolution cryo-EM structure of a small protein bound to an imaging scaffold.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
62 citing papers in PubMed.
- EXPECTATION-MAXIMIZATION FOR STRUCTURE DETERMINATION DIRECTLY FROM CRYO-EM MICROGRAPHS.Inverse problems and imaging (Springfield, Mo.) · 2027Article
- Mapping the Structure and Conformational Landscape of the 10-23 DNAzyme.ACS chemical biology · 2026Article
- High-resolution cryo-EM structures of small protein-ligand complexes near the theoretical size limit.Nature communications · 2026Article
- Trimbody with rigid AI-designed scaffolds enables atomic-resolution cryo-EM structure determination of small proteins.Nature communications · 2026Article
- Strategic advances for cryo-EM structural studies of small (<100 kDa) GPCRs.Communications biology · 2026Review
- Acoustically seeded fabrication of a DNA tesseract into a conductive wire.Nucleic acids research · 2025Article
- The mechanism of pathogenic αProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural determination of small proteins by cryo-EM using a coiled coil module strategy.Scientific reports · 2025Article
- Structures of a synthetic antibody selected against and bound to the C-terminal domain of Clostridium perfringens enterotoxin.Protein science : a publication of the Protein Society · 2025Article
- Computational design of bifaceted protein nanomaterials.Nature materials · 2025Article
- Disulfide-constrained Fabs overcome target size limitation for high-resolution single particle cryoEM.Nature communications · 2025Article
- Assignment-Free Determination of Ligand Binding Sites in Proteins by Solid-State NMR.Journal of the American Chemical Society · 2025Article
- Local structural flexibility drives oligomorphism in computationally designed protein assemblies.Nature structural & molecular biology · 2025Article
- A novel "bio-tag" for cryo-EM studies based on the small, electron-dense protein Csp1.Biophysical journal · 2025Article
- Article
- Unraveling atomic complexity from frozen samples.Structural dynamics (Melville, N.Y.) · 2025Article
- Activation and inhibition of sirtuins: From bench to bedside.Medicinal research reviews · 2025Review
- An immobilized antibody-based affinity grid strategy for on-grid purification of target proteins enables high-resolution cryo-EM.Communications biology · 2024Article
- Mitigating the Blurring Effect of CryoEM Averaging on a Flexible and Highly Symmetric Protein Complex through Sub-Particle Reconstruction.International journal of molecular sciences · 2024Article
- X-ray crystal structure of a designed rigidified imaging scaffold in the ligand-free conformation.Acta crystallographica. Section F, Structural biology communications · 2024Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Proteins smaller than about 50 kDa are currently too small to be imaged at high resolution by cryo-electron microscopy (cryo-EM), leaving most protein molecules in the cell beyond the reach of this powerful structural technique. Here we use a designed protein scaffold to bind and symmetrically display 12 copies of a small 26 kDa protein, green fluorescent protein (GFP). We show that the bound cargo protein is held rigidly enough to visualize it at a resolution of 3.8 Å by cryo-EM, where specific structural features of the protein are visible. The designed scaffold is modular and can be modified through modest changes in its amino acid sequence to bind and display diverse proteins for imaging, thus providing a general method to break through the lower size limitation in cryo-EM.
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Registered trials
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