| MWexperimental | 50 | kDa |
| MWexpected | 23 | kDa |
| VPorod | 127 | nm3 |
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log I(s)
5.09×100
5.09×10-1
5.09×10-2
5.09×10-3
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s, nm-1
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The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction.
Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S, iScience 27(12):111259 (2024) Europe PMCSASDVQ7 – PABL2 (Partner and localizer of BRCA2) L24A mutant
Partner and localizer of BRCA2 (L24A)|
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Fits and models
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Rg, nm
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Synchrotron SAXS
data from solutions of
PABL2 (Partner and localizer of BRCA2) L24A mutant
in
20 mM HEPES, 160 mM NaCl, 0.5 mM TCEP pH 7.5, pH 7.5
were collected
on the
ID7A1 BioSAXS / HP-Bio Beamline beam line
at the Cornell High Energy Synchrotron Source (CHESS) storage ring
(Ithaca, NY, USA)
using a Eiger 4M detector
at a sample-detector distance of 1.8 m and
at a wavelength of λ = 0.1097 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
One solute concentration of 5.10 mg/ml was measured
at 23°C.
2199 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.
REGALS-separated main component profile from SEC-SAXS experiment measuring PABL2 L24A mutant. NOTE: There is a significant inconsistency between the calculated MW from sequence of the monomer (23 kDa) and the quoted experimental MW (50 kDa). CAUTION: The X-ray exposure time is unlikely to be 2199 seconds. |
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