| MWexperimental | 40 | kDa |
| MWexpected | 53 | kDa |
| VPorod | 80 | nm3 |
|
log I(s)
9.50×100
9.50×10-1
9.50×10-2
9.50×10-3
|
s, nm-1
|
Direct interaction of DNA repair protein tyrosyl DNA phosphodiesterase 1 and the DNA ligase III catalytic domain is regulated by phosphorylation of its flexible N-terminus.
Rashid I, Hammel M, Sverzhinsky A, Tsai MS, Pascal JM, Tainer JA, Tomkinson AE, J Biol Chem :100921 (2021) Europe PMCSASDJP2 – Truncated tyrosyl-DNA phosphodiesterase 1 (TDP1 149-608)
Tyrosyl-DNA phosphodiesterase 1 (149-608)|
|
|
Fits and models
|
|
|
Synchrotron SAXS data from solutions of truncated tyrosyl-DNA phosphodiesterase 1 (TDP1 149-608) in 200 mM NaCl, 20 mM Tris-HCl, pH 7.5, 2% glycerol, were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 2.1 m and at a wavelength of λ = 0.1127 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 2 mg/ml was injected at a 0.50 ml/min flow rate onto a Shodex KW402.5-4F column at 20°C. 600 successive 3 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.
|
|
|||||||||||||||||||||||||||||||||