A prion-like domain is required for phase separation and chloroplast RNA processing during cold acclimation in Arabidopsis.

Legen J, Lenzen B, Kachariya N, Feltgen S, Gao Y, Mergenthal S, Weber W, Klotzsch E, Zoschke R, Sattler M, Schmitz-Linneweber C, Plant Cell (2024) Europe PMC

SASDT92 – Prion-like domain of 29 kDa chloroplastic ribonucleoprotein measured at at 298 K from Arabidopsis thaliana (Mouse-ear cress)

29 kDa ribonucleoprotein, chloroplastic
MWexperimental 8 kDa
MWexpected 8 kDa
VPorod 19 nm3
log I(s) 4.64×10-1 4.64×10-2 4.64×10-3 4.64×10-4
29 kDa ribonucleoprotein, chloroplastic small angle scattering data  s, nm-1
ln I(s)
29 kDa ribonucleoprotein, chloroplastic Guinier plot ln 4.64×10-1 Rg: 2.1 nm 0 (2.1 nm)-2 s2
29 kDa ribonucleoprotein, chloroplastic Kratky plot 1.104 0 3 sRg
29 kDa ribonucleoprotein, chloroplastic pair distance distribution function Rg: 2.3 nm 0 Dmax: 9.2 nm

Data validation

There are no models related to this curve.

SAXS data from solutions of the prion-like domain from 29 kDa chloroplastic ribonucleoprotein in 20 mM sodium phosphate, 30 mM NaCl, pH 6.2 were collected using a Rigaku BioSAXS-1000 instrument (Technische Universität München, Garching, Germany) equipped with a Pilatus 100K detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.155 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.00 mg/ml was measured at 25°C. Eight successive 900 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.

29 kDa ribonucleoprotein, chloroplastic (PLD of CP29A)
Mol. type   Protein
Organism   Arabidopsis thaliana
Olig. state   Monomer
Mon. MW   7.7 kDa
UniProt   Q43349 (176-254)
Sequence   FASTA