Dystrophin SAXS data

Raphael Dos Santos Morais.

SASDF25 – R16-24 del45-55 human dystrophin fragment

Human dystrophin central domain R16-24 del45-55 fragment
MWexperimental 61 kDa
MWexpected 58 kDa
log I(s) 1.03×100 1.03×10-1 1.03×10-2 1.03×10-3
Human dystrophin central domain R16-24 del45-55 fragment small angle scattering data  s, nm-1
ln I(s)
Human dystrophin central domain R16-24 del45-55 fragment Guinier plot ln 1.03×100 Rg: 4.7 nm 0 (4.7 nm)-2 s2
(sRg)2I(s)/I(0)
Human dystrophin central domain R16-24 del45-55 fragment Kratky plot 1.104 0 √3 sRg
p(r)
Human dystrophin central domain R16-24 del45-55 fragment pair distance distribution function Rg: 5.2 nm 0 Dmax: 18.3 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of the R16-24 del45-55 human dystrophin fragment in NaP 20 mM, NaCl 300 mM, EDTA 1 mM, glycerol 2%, pH 7.5 were collected using size-exclusion chromatography SAXS (SEC-SAXS) on the SWING beam line at SOLEIL (Saint-Aubin, France) using a CCD AVIEX PCCD170170 detector at a sample-detector distance of 1.8 m and at a wavelength of λ = 0.1033 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

SEC-SAXS was performed at 20°C using the following parameters: Column: BioSEC5-500Å (4.6 mm id * 300 mm); Flow rate: 0.2 mL/min; Sample injection concentration: ~8 mg/mL; Injection volume: 50μL. The data were collected through the SEC peak of the protein as a series of 21 x 1.5 second exposures. The experimental molecular weight was determined from the volume of correlation, Vc.

Human dystrophin central domain R16-24 del45-55 fragment
Mol. type   Protein
Olig. state   Monomer
Mon. MW   58.1 kDa
 
UniProt   P11532 (1990-3040)
Sequence   FASTA