Structural characterization of beta-sheeted oligomers formed on the pathway of oxidative prion protein aggregation in vitro.

Redecke L, von Bergen M, Clos J, Konarev PV, Svergun DI, Fittschen UE, Broekaert JA, Bruns O, Georgieva D, Mandelkow E, Genov N, Betzel C, J Struct Biol 157(2):308-20 (2007) Europe PMC

SASDMA7 – Prion protein aggregate in solution

Major prion protein
MWexperimental 405 kDa
MWexpected 664 kDa
VPorod 3320 nm3
log I(s) 1.27×105 1.27×104 1.27×103 1.27×102
Major prion protein small angle scattering data  s, nm-1
ln I(s)
Major prion protein Guinier plot ln 1.28×105 Rg: 9.8 nm 0 (9.8 nm)-2 s2
(sRg)2I(s)/I(0)
Major prion protein Kratky plot 1.104 0 √3 sRg
p(r)
Major prion protein pair distance distribution function Rg: 10.0 nm 0 Dmax: 32 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Major prion protein DAMMIN model
Synchrotron SAXS data from solutions of Prion protein aggregate in solution in 5 mM sodium acetate, pH 5 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a MAR 345 Image Plate detector at a sample-detector distance of 2.4 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 2.5 and 5 mg/ml were measured at 25°C. Two successive 120 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Tags: X33
Major prion protein (Prion aggregate)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   24-mer
Mon. MW   27.7 kDa
 
UniProt   P04156 (1-253)
Sequence   FASTA