| MWexperimental | 241 | kDa |
| MWexpected | 235 | kDa |
| VPorod | 431 | nm3 |
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log I(s)
8.89×10-2
8.89×10-3
8.89×10-4
8.89×10-5
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s, nm-1
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Integrative structural analysis of NF45-NF90 heterodimers reveals architectural rearrangements and oligomerization on binding dsRNA.
Winterbourne S, Jayachandran U, Zou J, Rappsilber J, Granneman S, Cook AG, Nucleic Acids Res 53(6) (2025) Europe PMCSASDUF5 – Interleukin enhancer-binding factor 3 (1-591) and Interleukin enhancer-binding factor 2 (1-390) heterodimer complex oligomerised along 25mer of dsRNA in a 4:1 ratio
Interleukin enhancer-binding factor 2Interleukin enhancer-binding factor 3
25-mer dsRNA
Interleukin enhancer-binding factor 2
Interleukin enhancer-binding factor 3
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Fits and models
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Synchrotron SAXS
data from solutions of
Interleukin enhancer-binding factor 3 (1-591) and Interleukin enhancer-binding factor 2 (1-390) heterodimer complex oligomerised along 25mer of dsRNA in a 4:1 ratio
in
20 mM HEPES, 150 mM NaCl, 1 mM DTT, pH 7.5
were collected
on the
B21 beam line
at the Diamond Light Source storage ring
(Didcot, UK)
using a Eiger 4M detector
at a sample-detector distance of 3.7 m and
at a wavelength of λ = 0.09464 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 60.00 μl sample
at 5.5 mg/ml was injected at a 0.07 ml/min flow rate
onto a Cytiva Superdex 200 Increase 3.2/300 column
at 15°C.
600 successive
0.005 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.
CAUTION: The DAMMIN model displayed in this entry shows a particle shape/volume calculated using a single average scattering length density whereas the complex is composed of two regions of different average scattering length density - protein and RNA. |
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