| MWexperimental | 670 | kDa |
| MWexpected | 622 | kDa |
| VPorod | 1490 | nm3 |
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log I(s)
1.97×10-1
1.97×10-2
1.97×10-3
1.97×10-4
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s, nm-1
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Deciphering cellular and molecular determinants of human DPCD protein in complex with RUVBL1/RUVBL2 AAA-ATPases.
Dos Santos Morais R, Santo PE, Ley M, Schelcher C, Abel Y, Plassart L, Deslignière E, Chagot ME, Quinternet M, Paiva ACF, Hessmann S, Morellet N, M F Sousa P, Vandermoere F, Bertrand E, Charpentier B, Bandeiras TM, Plisson-Chastang C, Verheggen C, Cianférani S, Manival X, J Mol Biol :167760 (2022) Europe PMCSASDFG5 – His-RuvBl1/RuvBl2 dodecamer
RuvB-like 1RuvB-like 2
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Fits and models
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Synchrotron SAXS data from solutions of the His-RuvBl1/RuvBl2 dodecamer in 20 mM HEPES, 150 mM NaCl, 1% glycerol, 5 mM TCEP, pH 7.5 were collected using size-exclusion chromatography SAXS (SEC-SAXS) on the SWING beam line at SOLEIL (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.1033 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). SEC-SAXS was performed at 15°C using the following parameters: Column: BioSEC5-500A (4.6 mm id * 300 mm); Flow rate: 0.3 mL/min; Sample injection concentration: 6 mg/mL; Injection volume: 50 μL. The data were collected through the SEC peak of the protein as a series of 17 x 1 second exposures. Each unsubtracted data frame was normalised to the intensity of the transmitted beam and radially averaged and the scattering of an appropriate solvent-blank was subtracted. The resulting subtracted frames were scaled and averaged to generate the final SAXS profile displayed in this entry.
The experimental molecular weight was determined from SEC-RALS/LALS experiment (670 kDa). |
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