Therapeutic approaches to ApoE

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

SASDG88 – Apolipoprotein E2 bound to 12 µM Suramin

Apolipoprotein E2
Suramin
MWexperimental 179 kDa
MWexpected 140 kDa
log I(s) 4.80×10-1 4.80×10-2 4.80×10-3 4.80×10-4
Apolipoprotein E2 Suramin small angle scattering data  s, nm-1
ln I(s)
Apolipoprotein E2 Suramin Guinier plot ln 4.80×10-1 Rg: 6.1 nm 0 (6.1 nm)-2 s2
(sRg)2I(s)/I(0)
Apolipoprotein E2 Suramin Kratky plot 1.104 0 √3 sRg
p(r)
Apolipoprotein E2 Suramin pair distance distribution function Rg: 6.2 nm 0 Dmax: 20.3 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Apolipoprotein E2 bound to 12 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.

ApoE2 + 12 µM Suramin

Apolipoprotein E2 (ApoE2)
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