The structure of the apolipoprotein A-I monomer provides insights into its oligomerisation and lipid-binding mechanisms

Tou H, Rosenes Z, Khandokar Y, Zlatic C, Metcalfe R, Mok Y, Morton C, Gooley P, Griffin M, Journal of Molecular Biology :169394 (2025) DOI

SASDUA9 – Apolipoprotein A-I monomer, C-terminally truncated, triply methionine-oxidised

Apolipoprotein A-I
MWexperimental 21 kDa
MWexpected 22 kDa
VPorod 32 nm3
log I(s) 1.19×10-2 1.19×10-3 1.19×10-4 1.19×10-5
Apolipoprotein A-I small angle scattering data  s, nm-1
ln I(s)
Apolipoprotein A-I Guinier plot ln 1.20×10-2 Rg: 2.5 nm 0 (2.5 nm)-2 s2
(sRg)2I(s)/I(0)
Apolipoprotein A-I Kratky plot 1.104 0 3 sRg
p(r)
Apolipoprotein A-I pair distance distribution function Rg: 2.5 nm 0 Dmax: 8 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of triply methionine-oxidised, C-terminally truncated Apolipoprotein A-I in 20 mM Tris, 150 mM NaCl, 0.1% sodium azide, pH 7.4 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus3 S 2M detector at a wavelength of λ = 0.1078 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 20°C. 13 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.

Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN

Apolipoprotein A-I (3MetO apoA-I)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   21.6 kDa
 
UniProt   P02647 (25-208)
Sequence   FASTA