| MWI(0) | 54 | kDa |
| MWexpected | 55 | kDa |
| VPorod | 107 | nm3 |
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log I(s)
3.24×10-1
3.24×10-2
3.24×10-3
3.24×10-4
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s, nm-1
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Rev7 dimerization is important for assembly and function of the Rev1/PolĪ¶ translesion synthesis complex.
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM, Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018) Europe PMCSASDC39 – Human Rev7 dimer in complex with Rev3 peptide @ 9.1mg/mL
Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunit
DNA polymerase zeta catalytic subunit
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Fits and models
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Synchrotron SAXS
data from solutions of
Human Rev7 dimer in complex with Rev3 peptide @ 9.1mg/mL
in
20 mM HEPES, 10 mM DTT, 5% glycerol, pH 8
were collected
on the
G1 beam line
at the Cornell High Energy Synchrotron Source (CHESS) storage ring
(Ithaca, NY, USA)
using a Finger Lakes CCD detector
at a wavelength of λ = 0.1267 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
One solute concentration of 9.10 mg/ml was measured
at 4°C.
10 successive
1 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.
Model was created by mapping the dimer interface by mutagenesis (9 residues identified) and then docking the dimer with HADDOCK and the mutations. SAXS/WAXS was used for cross-validation. |
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