| MWexperimental | 54 | kDa |
| MWexpected | 54 | kDa |
| VPorod | 103 | nm3 |
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log I(s)
3.88×102
3.88×101
3.88×100
3.88×10-1
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s, nm-1
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A key interaction with RPA orients XPA in NER complexes.
Topolska-Woś AM, Sugitani N, Cordoba JJ, Le Meur KV, Le Meur RA, Kim HS, Yeo JE, Rosenberg D, Hammel M, Schärer OD, Chazin WJ, Nucleic Acids Res (2020) Europe PMCSASDH44 – 3' Complex of XPA-DBD and RPA70AB
DNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunit
3-prime Nucleotide Excision Repair Junction Model Substrate
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Fits and models
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Synchrotron SAXS data from solutions of 3' Complex of XPA-DBD and RPA70AB in 20 mM Tris, 150 mM NaCl, 2% glycerol, 1 mM DTT, 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 1.5 m and at a wavelength of λ = 0.103 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 was injected at a 0.50 ml/min flow rate onto a Shodex LW-803 column at 20°C. Data measured from solute-free fractions and the sample-elution peak were normalized to the intensity of the transmitted beam and radially averaged. The scattering of the solvent-blank was subtracted from the sample peak data produce the data displayed in this entry.
Storage temperature = UNKNOWN. Number of frames = UNKNOWN |
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