| MWexperimental | 64 | kDa |
| MWexpected | 63 | kDa |
| VPorod | 76 | nm3 |
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log I(s)
2.23×101
2.23×100
2.23×10-1
2.23×10-2
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s, nm-1
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Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering.
Kaur G, Ren R, Hammel M, Horton JR, Yang J, Cao Y, He C, Lan F, Lan X, Blobel GA, Blumenthal RM, Zhang X, Cheng X, Nucleic Acids Res (2023) Europe PMCSASDQH5 – Zinc finger protein 410 (ZNF410 full length) bound to DNA
Zinc finger protein 410DNA (Zinc finger protein 410 recognition sequence)
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Fits and models
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Synchrotron SAXS data from solutions of ZNF410 (full length) bound to DNA in 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, 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 55.00 μl sample at 4 mg/ml was injected at a 0.50 ml/min flow rate onto a Shodex KW-800 series column at 20°C. 30 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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