Therapeutic approaches to ApoE

Lucas Kraft, University of Sussex PhD thesis 2019 (2019) URL

SASDGT8 – Apolipoprotein E4 (methylated) bound to 37 µM Suramin

Apolipoprotein E4
Suramin
MWexperimental 168 kDa
MWexpected 140 kDa
log I(s) 4.40×10-1 4.40×10-2 4.40×10-3 4.40×10-4
Apolipoprotein E4 Suramin small angle scattering data  s, nm-1
ln I(s)
Apolipoprotein E4 Suramin Guinier plot ln 4.40×10-1 Rg: 5.8 nm 0 (5.8 nm)-2 s2
(sRg)2I(s)/I(0)
Apolipoprotein E4 Suramin Kratky plot 1.104 0 √3 sRg
p(r)
Apolipoprotein E4 Suramin pair distance distribution function Rg: 6.0 nm 0 Dmax: 19.6 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Apolipoprotein E4 (methylated) bound to 37 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 (methylated) + 37 µM Suramin

Apolipoprotein E4 (ApoE4)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Tetramer
Mon. MW   34.7 kDa
 
UniProt   P02649 (19-317)
Sequence   FASTA
 
Suramin
Mol. type   Other
Olig. state   Monomer
Mon. MW   1.3 kDa
Chemical formula