ArticleStructure (London, England : 1993)2012
Fabs enable single particle cryoEM studies of small proteins.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.
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Who cites it
110 citing papers in PubMed.
- EXPECTATION-MAXIMIZATION FOR STRUCTURE DETERMINATION DIRECTLY FROM CRYO-EM MICROGRAPHS.Inverse problems and imaging (Springfield, Mo.) · 2027Article
- Flower Delivery: The Emergence of FLOWER (FWE) as a Multifunctional Regulator of Endo-Lysosome-Related Organelle Trafficking Across Cell Types.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Optimized bacterial expression of a synthetic BRIL antibody.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Trimbody with rigid AI-designed scaffolds enables atomic-resolution cryo-EM structure determination of small proteins.Nature communications · 2026Article
- Cryo-EM structures of antibodies elicited by germline-targeting HIV MPER epitope scaffolds.Cell reports · 2026Article
- Antibody-enabled structural biology and AI-driven antibody design.Frontiers in pharmacology · 2026Review
- Design and Optimization of BRIL Fusion Constructs for Membrane Protein Cryo-EM Studies.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Covalently constrained 'Di-Gembodies' enable parallel structure solutions by cryo-EM.Nature chemical biology · 2026Article
- Dynamic structures of a membrane transporter in native cellular membranes.Science advances · 2025Article
- Disulfide-constrained Fabs overcome target size limitation for high-resolution single particle cryoEM.Nature communications · 2025Article
- Cryo-EM structures of HCV E2 glycoprotein bound to neutralizing and non-neutralizing antibodies determined using bivalent Fabs as fiducial markers.Communications biology · 2025Article
- Inactive structures of the vasopressin V2 receptor reveal distinct binding modes for Tolvaptan and Mambaquaretin toxin.Nature communications · 2025Article
- Unraveling atomic complexity from frozen samples.Structural dynamics (Melville, N.Y.) · 2025Article
- A fiducial-assisted strategy compatible with resolving small MFS transporter structures in multiple conformations using cryo-EM.Nature communications · 2025Article
- An Overview of Epitopes and Methods for Antibody Epitope Mapping.Methods in molecular biology (Clifton, N.J.) · 2025Review
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- Apolipoprotein E secreted by astrocytes forms antiparallel dimers in discoidal lipoproteins.Neuron · 2024Article
- Sample Preparation for Electron Cryo-Microscopy of Macromolecular Machines.Advances in experimental medicine and biology · 2024Article
- CryoEM structure of a therapeutic antibody (favezelimab) bound to human LAG3 determined using a bivalent Fab as fiducial marker.Structure (London, England : 1993) · 2023Article
50 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
20 authors.
Funding
Abstract
In spite of its recent achievements, the technique of single particle electron cryomicroscopy (cryoEM) has not been widely used to study proteins smaller than 100 kDa, although it is a highly desirable application of this technique. One fundamental limitation is that images of small proteins embedded in vitreous ice do not contain adequate features for accurate image alignment. We describe a general strategy to overcome this limitation by selecting a fragment antigen binding (Fab) to form a stable and rigid complex with a target protein, thus providing a defined feature for accurate image alignment. Using this approach, we determined a three-dimensional structure of an ∼65 kDa protein by single particle cryoEM. Because Fabs can be readily generated against a wide range of proteins by phage display, this approach is generally applicable to study many small proteins by single particle cryoEM.
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