Apolipoprotein E project

Lucas Kraft.

SASDGP8 – Apolipoprotein E4 (K143A K146A) mutant bound to12 µM Suramin

Apolipoprotein E4 (K143A K146A) mutant
Suramin
MWexperimental 156 kDa
MWexpected 140 kDa
log I(s) 3.50×10-1 3.50×10-2 3.50×10-3 3.50×10-4
Apolipoprotein E4 (K143A K146A) mutant Suramin small angle scattering data  s, nm-1
ln I(s)
Apolipoprotein E4 (K143A K146A) mutant Suramin Guinier plot ln 3.50×10-1 Rg: 6.0 nm 0 (6.0 nm)-2 s2
(sRg)2I(s)/I(0)
Apolipoprotein E4 (K143A K146A) mutant Suramin Kratky plot 1.104 0 3 sRg
p(r)
Apolipoprotein E4 (K143A K146A) mutant Suramin pair distance distribution function Rg: 6.1 nm 0 Dmax: 20.2 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Apolipoprotein E4 (K143A K146A) mutant bound to12 µM Suramin in 20 mM HEPES, 300 mM NaCl, 1 mM TCEP, pH 8 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Pilatus 2M detector at a sample-detector distance of 4.0 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.00 mg/ml was measured at 20°C. 28 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.

ApoE4 (K143A K146A) + 12 µM Suramin

Apolipoprotein E4 (K143A K146A) mutant (ApoE4 (K143A K146A))
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Tetramer
Mon. MW   34.6 kDa
 
UniProt   P02649 (19-317)
Sequence   FASTA
 
Suramin
Mol. type   Other
Olig. state   Monomer
Mon. MW   1.3 kDa
Chemical formula