Interactions of ataxin-3 with its molecular partners in the protein machinery that sorts protein aggregates to the aggresome.

Bonanomi M, Mazzucchelli S, D'Urzo A, Nardini M, Konarev PV, Invernizzi G, Svergun DI, Vanoni M, Regonesi ME, Tortora P, Int J Biochem Cell Biol 51:58-64 (2014) Europe PMC

SASDLJ5 – Aggregation state of tubulin protein

Tubulin alpha-1A chain
MWexperimental 280 kDa
MWexpected 50 kDa
VPorod 340 nm3
log I(s) 1.97×102 1.97×101 1.97×100 1.97×10-1
Tubulin alpha-1A chain small angle scattering data  s, nm-1
ln I(s)
Tubulin alpha-1A chain Guinier plot ln 1.97×102 Rg: 7 nm 0 (7 nm)-2 s2
(sRg)2I(s)/I(0)
Tubulin alpha-1A chain Kratky plot 1.104 0 √3 sRg
p(r)
Tubulin alpha-1A chain pair distance distribution function Rg: 7.1 nm 0 Dmax: 25 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Tubulin alpha-1A chain DAMMIN model
Synchrotron SAXS data from solutions of tubulin in phosphate buffered saline (PBS), pH 7.4 were collected on the EMBL X33 beam line at DORIS III (DESY, Hamburg, Germany) using a Pilatus 1M-W detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 7.50 mg/ml was measured at 10°C. Four successive 30 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.

Tags: X33
Tubulin alpha-1A chain (Tubulin)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   50.1 kDa
 
UniProt   Q71U36 (1-451)
Sequence   FASTA