| MWexperimental | 123 | kDa |
| MWexpected | 127 | kDa |
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log I(s)
2.76×10-2
2.76×10-3
2.76×10-4
2.76×10-5
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s, nm-1
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Evolutionary conservation of the structure and function of meiotic Rec114-Mei4 and Mer2 complexes.
Daccache D, De Jonge E, Liloku P, Mechleb K, Haddad M, Corthaut S, Sterckx YG, Volkov AN, Claeys Bouuaert C, Genes Dev 37(11-12):535-553 (2023) Europe PMCSASDSU2 – Mus musculus Iho1 coiled-coiled with N-terminal SUMO-tag
Interactor of HORMAD1 protein 1 (M198V, V230I)|
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Fits and models
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Synchrotron SAXS
data from solutions of
Mus musculus Iho1 coiled-coiled with N-terminal SUMO-tag
in
25 mM HEPES-NaOH, 500 mM NaCl, 5 mM EDTA, 5% glycerol, 1 mM DTT, pH 7.5
were collected
on the
SWING beam line
at the SOLEIL storage ring
(Saint-Aubin, France)
using a Eiger 4M detector
at a sample-detector distance of 2 m and
at a wavelength of λ = 0.099 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 90.00 μl sample
at 19.4 mg/ml was injected at a 0.20 ml/min flow rate
onto a Shodex KW404-4F column
at 15°C.
960 successive
0.990 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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