| MWexperimental | 180 | kDa |
| MWexpected | 69 | kDa |
| VPorod | 675 | nm3 |
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log I(s)
1.00×104
1.00×103
1.00×102
1.00×101
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s, nm-1
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An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex.
Hammel M, Rashid I, Sverzhinsky A, Pourfarjam Y, Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE, Nucleic Acids Res (2020) Europe PMCSASDJ82 – DNA repair protein XRCC1 - DNA Ligase IIIα complex
DNA repair protein XRCC1DNA ligase 3 (DNA ligase III alpha)
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Fits and models
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Synchrotron SAXS data from solutions of the DNA repair protein XRCC1 - DNA Ligase IIIα complex in 50 mM Tris-HCl, pH 7.5, 100 mM NaCl, 5 mM MgCl₂, 0.2 mM PMSF, 1 mM benzamidine, 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 4 mg/ml was injected at a 0.50 ml/min flow rate onto a Shodex LW-803 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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