Apolipoprotein E project

Lucas Kraft.

SASDGP9 – Mutant Apolipoprotein E4 (K143A K146A) bound to 1 mM Suramin (SEC-SAXS)

Apolipoprotein E4 (K143A K146A) mutant
Suramin
MWexperimental 145 kDa
MWexpected 140 kDa
log I(s) 2.03×10-1 2.03×10-2 2.03×10-3 2.03×10-4
Apolipoprotein E4 (K143A K146A) mutant Suramin small angle scattering data  s, nm-1
ln I(s)
Apolipoprotein E4 (K143A K146A) mutant Suramin Guinier plot ln 2.04×10-1 Rg: 5.4 nm 0 (5.4 nm)-2 s2
(sRg)2I(s)/I(0)
Apolipoprotein E4 (K143A K146A) mutant Suramin Kratky plot 1.104 0 3 sRg
p(r)
Apolipoprotein E4 (K143A K146A) mutant Suramin pair distance distribution function Rg: 5.5 nm 0 Dmax: 18.3 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 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 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 preequilibrated with 1 mM Suramin and then gel-filtered in 20 mM HEPES, 300 mM NaCl, 1 mM TCEP, pH 8.0.

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
 
Suramin
Mol. type   Other
Olig. state   Monomer
Mon. MW   1.3 kDa
Chemical formula