Multiscale characterization reveals oligomerization dependent phase separation of primer-independent RNA polymerase nsp8 from SARS-CoV-2.

Xu J, Jiang X, Zhang Y, Dong Y, Ma C, Jiang H, Zuo T, Chen R, Ke Y, Cheng H, Wang H, Liu J, Commun Biol 5(1):925 (2022) Europe PMC

SASDP76 – SARS-CoV-2 non-structural protein 8 (nsp8, dimer) in 1000 mM NaCl buffer

Replicase polyprotein 1a (Non-structural protein 8, SARS-CoV-2)
MWexperimental 44 kDa
MWexpected 44 kDa
VPorod 100 nm3
log I(s) 6.49×10-1 6.49×10-2 6.49×10-3 6.49×10-4
Replicase polyprotein 1a (Non-structural protein 8, SARS-CoV-2) small angle scattering data  s, nm-1
ln I(s)
Replicase polyprotein 1a (Non-structural protein 8, SARS-CoV-2) Guinier plot ln 6.49×10-1 Rg: 3.8 nm 0 (3.8 nm)-2 s2
(sRg)2I(s)/I(0)
Replicase polyprotein 1a (Non-structural protein 8, SARS-CoV-2) Kratky plot 1.104 0 √3 sRg
Dmax: 14 nm

Data validation

There are no models related to this curve.

SANS data from solutions of SARS-CoV-2 non-structural protein 8 in 20 mM HEPES pH 7.4, 1000 mM NaCl, were collected on the BL01-Small Angle Neutron Scattering instrument (China Spallation Neutron Source, Dongguan, China) using a LND detector at a sample-detector distance of 4 m and at a wavelength of λ = 0.95 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 16°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Neutron Exposure time = UNKNOWN.

Replicase polyprotein 1a (Non-structural protein 8, SARS-CoV-2) (nsp8)
Mol. type   Protein
Organism   Severe acute respiratory syndrome coronavirus 2
Olig. state   Dimer
Mon. MW   21.9 kDa
 
UniProt   P0DTC1 (3943-4140)
Sequence   FASTA