| MWexperimental | 21 | kDa |
| MWexpected | 22 | kDa |
| VPorod | 41 | nm3 |
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log I(s)
4.89×10-2
4.89×10-3
4.89×10-4
4.89×10-5
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s, nm-1
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Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain.
Viola G, Trivellato D, Laitaoja M, Jänis J, Felli IC, D'Onofrio M, Mollica L, Giachin G, Assfalg M, Proc Natl Acad Sci U S A 122(15):e2425831122 (2025) Europe PMCSASDV56 – Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to Ubiquitin at tau residue C317
Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)Polyubiquitin-B
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Fits and models
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Rg, nm
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Synchrotron SAXS data from solutions of microtubule-associated protein tau (lysine-rich four-repeat domain 4RD) synthetically linked to ubiquitin at tau amino acid C317 in 100 mM NaCl, pH 6.8 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.123972 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.00 mg/ml was measured at 20°C. 20 successive 0.050 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
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