| MWexperimental | 340 | kDa |
| MWexpected | 71 | kDa |
| VPorod | 790 | nm3 |
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log I(s)
1.03×102
1.03×101
1.03×100
1.03×10-1
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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 PMCSASDJR2 – DNA ligase 3 bound to tyrosyl-DNA phosphodiesterase 1 (LigIIIα/TDP1 complex)
DNA ligase 3 (DNA ligase III alpha)Tyrosyl-DNA phosphodiesterase 1
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Fits and models
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Synchrotron SAXS data from solutions of the LigIIIα/TDP1 complex in 200 mM NaCl, 40 mM HEPES, pH 7.5 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 3 mg/ml was injected at a 0.50 ml/min flow rate onto a Shodex KW-800 series 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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