| MWexperimental | 71 | kDa |
| MWexpected | 71 | kDa |
| VPorod | 110 | nm3 |
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log I(s)
1.79×101
1.79×100
1.79×10-1
1.79×10-2
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s, nm-1
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An intrinsically disordered transcription activation domain increases the DNA binding affinity and reduces the specificity of NFκB p50/RelA.
Baughman HER, Narang D, Chen W, Villagrán Suárez AC, Lee J, Bachochin MJ, Gunther TR, Wolynes PG, Komives EA, J Biol Chem :102349 (2022) Europe PMCSASDHB5 – RelA Homology Domain of p50/RelA heterodimer
NF-kappa-B p105 subunit 39-350Transcription factor p65 19-321
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Fits and models
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Synchrotron SAXS data from solutions of the Rel Homology Domian of p50/RelA heterodimer in 25 mM Tris.Cl, 150 mM NaCl, 1 mM DTT, 0.5 mM EDTA, 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 m and at a wavelength of λ = 0.127 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.3 and 5 mg/ml were measured at 10°C. 50 successive 15 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.
Storage temperature = UNKNOWN |
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