| MWexperimental | 37 | kDa |
| MWexpected | 40 | kDa |
| VPorod | 75 | nm3 |
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log I(s)
6.48×10-3
6.48×10-4
6.48×10-5
6.48×10-6
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s, nm-1
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Structural insights into the C-terminus of the histone-lysine N-methyltransferase NSD3 by small-angle X-ray scattering.
Belviso BD, Shen Y, Carrozzini B, Morishita M, di Luccio E, Caliandro R, Front Mol Biosci 11:1191246 (2024) Europe PMCSASDNK8 – The C-terminal region of histone-lysine N-methyltransferase NSD3: SET-PHD4 construct
Histone-lysine N-methyltransferase NSD3|
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Fits and models
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Synchrotron SAXS data from solutions of the C-terminal region of histone-lysine N-methyltransferase NSD3 (SET-PHD4 construct) in 0.5 M NaCl, 20 mM Tris-HCl, 5 mM DTT, pH 8.5 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 4.0 m and at a wavelength of λ = 0.1 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 1.6 mg/ml was injected at a 0.16 ml/min flow rate onto a Shodex KW402.5-4F column at 20°C. 200 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.
The individual (unsubtracted) SEC-SAXS data frames and all DAMMIF model reconstructions are included in the full entry zip archive. |
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