| MWexperimental | 21 | kDa |
| MWexpected | 22 | kDa |
| VPorod | 33 | nm3 |
|
log I(s)
1.03×103
1.03×102
1.03×101
1.03×100
|
s, nm-1
|
Conformational signatures induced by ubiquitin modification in the amyloid-associated tau repeat domain
Gabriele Giachin.SASDV66 – Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to Ubiquitin at tau residue C353
Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)Polyubiquitin-B
|
|
|
Fits and models
|
Rg, nm
|
|
Synchrotron SAXS data from solutions of microtubule-associated protein tau (lysine-rich four-repeat domain 4RD) synthetically linked to ubiquitin at tau amino acid C353 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 2.00 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.
|
|
||||||||||||||||||||||||||||||||||||||||||||||||||||||