Apolipoprotein E project

Lucas Kraft.

SASDGQ7 – Mutant Apolipoprotein E4 (K143A K146A) bound to 110 µg/mL heparin

Heparin
Apolipoprotein E4 (K143A K146A) mutant
MWexperimental 160 kDa
MWexpected 153 kDa
log I(s) 3.40×10-1 3.40×10-2 3.40×10-3 3.40×10-4
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 3.40×10-1 Rg: 6.1 nm 0 (6.1 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: 6.3 nm 0 Dmax: 21.2 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Mutant Apolipoprotein E4 (K143A K146A) bound to 110 µg/mL heparin 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) mutant + 110 µg/mL heparin. Molecular weight estimates are inaccurate due to heparin heterogeneity.

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