| MWI(0) | 131 | kDa |
| MWexpected | 132 | kDa |
| VPorod | 220 | nm3 |
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log I(s)
5.32×101
5.32×100
5.32×10-1
5.32×10-2
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s, nm-1
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Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair
Kim M, Kim H, D’Souza A, Gallagher K, Jeong E, Topolska-Wós A, Ogorodnik Le Meur K, Tsai C, Tsai M, Kee M, Tainer J, Yeo J, Chazin W, Schärer O, Proceedings of the National Academy of Sciences 119(34) (2022) DOISASDP24 – Complex of XPA1-239 and RPAΔ32NΔ70N complex engaged on 5’ss-ds DNA junction NER substrate
Replication protein A 14 kDa subunitDNA repair protein complementing XP-A cells
Replication protein A 70 kDa DNA-binding subunit
Replication protein A 32 kDa subunit
5-prime ss-ds DNA junction NER model substrate
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Fits and models
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Synchrotron SAXS data from solutions of 3' Complex of XPA and RPA in 20 mM Tris, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH 8.0 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.
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