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TitleDisulfide-constrained Fabs overcome target size limitation for high-resolution single particle cryoEM.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 8687, Year 2025
Publish dateSep 30, 2025
AuthorsJennifer E Kung / Matthew C Johnson / Dimitry Tegunov / Christine C Jao / Ping Wu / Angela Oh / May Lin / Jose M Daria / Christopher M Koth / Christopher P Arthur / Alexis Rohou / Jawahar Sudhamsu /
PubMed AbstractHigh-resolution protein structures are essential for understanding biological mechanisms and drug discovery. While cryoEM has revolutionized structure determination of large protein complexes, most ...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.
External linksNat Commun / PubMed:41027970 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 3.7 Å
Structure data

EMDB-71531: Angiopoietin-2 in complex with engineered conformationally rigid Fab 5A12.6DS, used for comparison with Fab 5A12.WT
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-71532: Angiopoietin-2 in complex with Fab 5A12.WT, used for comparison with Fab 5A12.6DS
Method: EM (single particle) / Resolution: 3.7 Å

Source
  • Homo sapiens (human)

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