A structural study of the cytoplasmic chaperone effect of 14-3-3 proteins on Ataxin-1.

Leysen S, Jane Burnley R, Rodriguez E, Milroy LG, Soini L, Adamski CJ, Nitschke L, Davis R, Obsil T, Brunsveld L, Crabbe T, Yahya Zoghbi H, Ottmann C, Martin Davis J, J Mol Biol :167174 (2021) Europe PMC

SASDLT3 – Ataxin-1 AXH-C

Ataxin-1
MWexperimental 56 kDa
MWexpected 55 kDa
VPorod 90 nm3
log I(s) 3.66×10-2 3.66×10-3 3.66×10-4 3.66×10-5
Ataxin-1 small angle scattering data  s, nm-1
ln I(s)
Ataxin-1 Guinier plot ln 3.66×10-2 Rg: 4.3 nm 0 (4.3 nm)-2 s2
(sRg)2I(s)/I(0)
Ataxin-1 Kratky plot 1.104 0 √3 sRg
p(r)
Ataxin-1 pair distance distribution function Rg: 4.4 nm 0 Dmax: 14.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Ataxin-1 AXH-C Rg histogram Rg, nm
Ataxin-1 EOM/RANCH model
Ataxin-1 EOM/RANCH model
Ataxin-1 EOM/RANCH model
Ataxin-1 EOM/RANCH model
Ataxin-1 EOM/RANCH model
Ataxin-1 EOM/RANCH model
Synchrotron SAXS data from solutions of ataxin-1 AXH-C in 20 mM HEPES, 150 mM NaCl, 2 mM DTT, pH 7.5 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Pilatus 2M detector 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 12.8 mg/ml was injected onto a Shodex KW403 column at 25°C. 3 second data frames were collected through the SEC elution (620 data frames, total). 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. Flow rate = UNKNOWN

Ataxin-1 (AXH-C)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   27.7 kDa
 
UniProt   P54253 (562-815)
Sequence   FASTA