R2SP

Raphael Dos Santos Morais.

SASDG22 – RuvB-like 1 and 2 dodecamer (His-RuvBL1/RuvBL2)

RuvB-like 1
RuvB-like 2
MWexperimental 761 kDa
MWexpected 622 kDa
VPorod 1550 nm3
log I(s) 3.02×10-1 3.02×10-2 3.02×10-3 3.02×10-4
RuvB-like 1 RuvB-like 2 small angle scattering data  s, nm-1
ln I(s)
RuvB-like 1 RuvB-like 2 Guinier plot ln 3.02×10-1 Rg: 6.3 nm 0 (6.3 nm)-2 s2
(sRg)2I(s)/I(0)
RuvB-like 1 RuvB-like 2 Kratky plot 1.104 0 3 sRg
p(r)
RuvB-like 1 RuvB-like 2 pair distance distribution function Rg: 6.3 nm 0 Dmax: 23.4 nm

Data validation


Fits and models


log I(s)
 s, nm-1
RuvB-like 1 RuvB-like 2 DAMMIF model

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: Agilent Bio SEC-5, 500Å (4.6 mm id * 300 mm); Flow rate: 0.3 mL/min; Sample injection concentration: 8.45 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 the volume of correlation, Vc.

Storage temperature = UNKNOWN

RuvB-like 1
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Hexamer
Mon. MW   51.8 kDa
 
UniProt   Q9Y265 (1-456)
Sequence   FASTA
 
RuvB-like 2
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Hexamer
Mon. MW   51.9 kDa
 
UniProt   Q9Y230 (1-463)
Sequence   FASTA