Apolipoprotein E project

Lucas Kraft.

SASDGB9 – Apolipoprotein E2 bound to 1 mM Suramin (SEC-SAXS)

Apolipoprotein E2
MWexperimental 148 kDa
MWexpected 140 kDa
log I(s) 2.80×10-1 2.80×10-2 2.80×10-3 2.80×10-4
Apolipoprotein E2 Suramin small angle scattering data  s, nm-1
ln I(s)
Apolipoprotein E2 Suramin Guinier plot ln 2.80×10-1 Rg: 5.1 nm 0 (5.1 nm)-2 s2
Apolipoprotein E2 Suramin Kratky plot 1.104 0 3 sRg
Apolipoprotein E2 Suramin pair distance distribution function Rg: 5.4 nm 0 Dmax: 18.3 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Apolipoprotein E2 bound to 1 mM Suramin (SEC-SAXS) 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). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 45.00 μl sample at 10 mg/ml was injected at a 0.16 ml/min flow rate onto a Shodex KW403-4F column at 20°C. 14 successive 3 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 at 10 mg/mL was preequilibrated with 1 mM Suramin and then gel-filtered in 20 mM HEPES, 300 mM NaCl, 1 mM TCEP, pH 8.0.

Apolipoprotein E2 (ApoE2)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Tetramer
Mon. MW   34.6 kDa
UniProt   P02649 (19-317)
Sequence   FASTA
Mol. type   Other
Olig. state   Monomer
Mon. MW   1.3 kDa
Chemical formula