ArticleProceedings of the National Academy of Sciences of the United States of America2018
Near-atomic cryo-EM imaging of a small protein displayed on a designed scaffolding system.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
What it found
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Who cites it
59 citing papers in PubMed, 100 citations in OpenAlex.
- Structural basis of the gating mechanism of the large-conductance mechanosensitive channel from Escherichia coli.Nature communications · 2026Article
- Modular Scaffold Crystals for Programmable Installation and Structural Observation of DNA-Binding Proteins.bioRxiv : the preprint server for biology · 2026Article
- Trimbody with rigid AI-designed scaffolds enables atomic-resolution cryo-EM structure determination of small proteins.Nature communications · 2026Article
- Acoustically seeded fabrication of a DNA tesseract into a conductive wire.Nucleic acids research · 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
- Local structural flexibility drives oligomorphism in computationally designed protein assemblies.Nature structural & molecular biology · 2025Article
- Article
- Rigid enlargement of sybodies with antibody fragments for cryo-EM analyses of small membrane proteins.Scientific reports · 2025Article
- Article
- A designed ankyrin-repeat protein that targets Parkinson's disease-associated LRRK2.The Journal of biological chemistry · 2024Article
- Cryo-electron microscopy for GPCR research and drug discovery in endocrinology and metabolism.Nature reviews. Endocrinology · 2024Review
- 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
- Article
- Macromolecular Cargo Encapsulation via In Vitro Assembly of Two-Component Protein Nanoparticles.Advanced healthcare materials · 2024Article
- Design of a symmetry-broken tetrahedral protein cage by a method of internal steric occlusion.Protein science : a publication of the Protein Society · 2024Article
- Rapid and automated design of two-component protein nanomaterials using ProteinMPNN.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Cryo-electron microscopy-based drug design.Frontiers in molecular biosciences · 2024Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Current single-particle cryo-electron microscopy (cryo-EM) techniques can produce images of large protein assemblies and macromolecular complexes at atomic level detail without the need for crystal growth. However, proteins of smaller size, typical of those found throughout the cell, are not presently amenable to detailed structural elucidation by cryo-EM. Here we use protein design to create a modular, symmetrical scaffolding system to make protein molecules of typical size suitable for cryo-EM. Using a rigid continuous alpha helical linker, we connect a small 17-kDa protein (DARPin) to a protein subunit that was designed to self-assemble into a cage with cubic symmetry. We show that the resulting construct is amenable to structural analysis by single-particle cryo-EM, allowing us to identify and solve the structure of the attached small protein at near-atomic detail, ranging from 3.5- to 5-Å resolution. The result demonstrates that proteins considerably smaller than the theoretical limit of 50 kDa for cryo-EM can be visualized clearly when arrayed in a rigid fashion on a symmetric designed protein scaffold. Furthermore, because the amino acid sequence of a DARPin can be chosen to confer tight binding to various other protein or nucleic acid molecules, the system provides a future route for imaging diverse macromolecules, potentially broadening the application of cryo-EM to proteins of typical size in the cell.
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Registered trials
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.