ArticleNature communications2025
Disulfide-constrained Fabs overcome target size limitation for high-resolution single particle cryoEM.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Cryogenic electron microscopy and coagulation factors.Current opinion in hematology · 2026Review
- SAKE-PP: A Spatial-Attention Equivariant Network for Accurate Ranking of Protein-Protein Interaction Models.JACS Au · 2026Article
- Designing Rigid Protein Fiducials to Visualize GPCR Conformational States.bioRxiv : the preprint server for biology · 2026Article
- 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
- Structural polymorphism of the antigenic loop in HBV surface antigen dictates binding of diverse neutralizing antibodies.Cell discovery · 2025Article
- A novel "bio-tag" for cryo-EM studies based on the small, electron-dense protein Csp1.Biophysical journal · 2025Article
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12 authors.
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Abstract
High-resolution protein structures are essential for understanding biological mechanisms and drug discovery. While cryoEM has revolutionized structure determination of large protein complexes, most disease-related proteins are small (<50 kDa) and challenging to resolve due to low signal-to-noise ratios and alignment difficulties. Current scaffold protein strategies increase target size but suffer from inherent flexibility, resulting in poorly resolved targets compared to scaffolds. We present an iteratively engineered molecular design transforming antibody fragments (Fabs) into conformationally Rigid Fabs that enable high-resolution structure determination of small proteins (~20 kDa). This design introduces strategic disulfide bonds, creating well-folded, rigidly constrained Fabs applicable across various species, frameworks, and chimeric constructs. Rigid Fabs enabled high-resolution cryoEM structures (2.3-2.5 Å) of two small proteins: Ang2 (26 kDa) and KRAS (21 kDa). Our disulfide-constrained Rigid Fab strategy provides a general approach for overcoming target size limitation of single-particle cryoEM.
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Registered trials
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