| MWexperimental | 64 | kDa |
| MWexpected | 71 | kDa |
| VPorod | 141 | nm3 |
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log I(s)
2.35×102
2.35×101
2.35×100
2.35×10-1
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s, nm-1
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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 PMCSASDJQ2 – Dephosphorylated tyrosyl-DNA phosphodiesterase 1 (TDP1-Ppi)
Tyrosyl-DNA phosphodiesterase 1 (dephosphorylated)|
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Fits and models
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Synchrotron SAXS data from solutions of dephosphorylated tyrosyl-DNA phosphodiesterase 1 (TDP1-Ppi) 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 10 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.
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