Apolipoprotein E project

Lucas Kraft.

SASDGN9 – Mutant Apolipoprotein E4 (K143A K146A) bound to 1 mg/mL heparin (SEC-SAXS)

Heparin
Apolipoprotein E4 (K143A K146A) mutant
MWexperimental 165 kDa
MWexpected 153 kDa
log I(s) 1.76×10-1 1.76×10-2 1.76×10-3 1.76×10-4
Heparin Apolipoprotein E4 (K143A K146A) mutant small angle scattering data  s, nm-1
ln I(s)
Heparin Apolipoprotein E4 (K143A K146A) mutant Guinier plot ln 1.77×10-1 Rg: 5.7 nm 0 (5.7 nm)-2 s2
(sRg)2I(s)/I(0)
Heparin Apolipoprotein E4 (K143A K146A) mutant Kratky plot 1.104 0 3 sRg
p(r)
Heparin Apolipoprotein E4 (K143A K146A) mutant pair distance distribution function Rg: 5.9 nm 0 Dmax: 19.8 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Mutant Apolipoprotein E4 (K143A K146A) bound to 1 mg/mL heparin (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. 11 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.

Mutant ApoE4 (K143A K146A) at 10 mg/mL was gel-filtered in 20 mM HEPES, 300 mM NaCl, 1 mM TCEP, 1 mg/mL heparin, pH 8.0.

Heparin
Mol. type   Other
Olig. state   Monomer
Mon. MW   15 kDa
Chemical formula
 
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