| MWI(0) | 45 | kDa |
| MWexpected | 44 | kDa |
| VPorod | 100 | nm3 |
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log I(s)
3.00×103
3.00×102
3.00×101
3.00×100
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s, nm-1
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Frameshift PQBP-1 mutants K192Sfs*7 and R153Sfs*41 implicated in X-linked intellectual disability form stable dimers.
Rahman SK, Okazawa H, Chen YW, J Struct Biol (2019) Europe PMCSASDEU6 – Polyglutamine-binding protein 1 p.Arg153Serfs*41 (PQBP-1 XLID mutant R153Sfs*41)
Polyglutamine-binding protein 1 p.Arg153Serfs*41|
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Fits and models
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Rg, nm
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Synchrotron SAXS data from solutions of polyglutamine-binding protein 1 p.Arg153Serfs*41 in phosphate-buffered saline, pH 7.4 were collected on the EMBL X33 beam line at the DORIS III storage ring (DESY, Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 7.3 mg/ml were measured at 10°C using an X-ray exposure time of 45 ms. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.
The entry displays the EOM ensemble Rg distributions and the fit to the data of the refined ensemble. The full EOM ensemble and log file describing the associated volume fractions is available for download in the full entry zip-archive. |
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