Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site.

Lee J, Worrall LJ, Vuckovic M, Rosell FI, Gentile F, Ton AT, Caveney NA, Ban F, Cherkasov A, Paetzel M, Strynadka NCJ, Nat Commun 11(1):5877 (2020) Europe PMC

SASDJH5 – SARS-CoV-2 Main Protease, P9T mutant

3C-like proteinase from SARS-CoV-2 replicase polyprotein 1a, PT9 mutant
MWexperimental 38 kDa
MWexpected 34 kDa
VPorod 54 nm3
log I(s) 1.22×100 1.22×10-1 1.22×10-2 1.22×10-3
3C-like proteinase from SARS-CoV-2 replicase polyprotein 1a, PT9 mutant small angle scattering data  s, nm-1
ln I(s)
3C-like proteinase from SARS-CoV-2 replicase polyprotein 1a, PT9 mutant Guinier plot ln 1.22×100 Rg: 2.4 nm 0 (2.4 nm)-2 s2
(sRg)2I(s)/I(0)
3C-like proteinase from SARS-CoV-2 replicase polyprotein 1a, PT9 mutant Kratky plot 1.104 0 √3 sRg
Dmax: 7.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
3C-like proteinase from SARS-CoV-2 replicase polyprotein 1a, PT9 mutant SREFLEX model
SAXS data from solutions of SARS-CoV-2 Main Protease, P9T mutant in 50 mM Tris, 1 mM DTT, 1 mM EDTA, pH 7.4 were collected using a Rigaku BioSAXS-2000 instrument (University of British Columbia, Vancouver, Canada) equipped with a HyPix-3000 detector at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.5 and 24.5 mg/ml were measured at 6°C. 12 successive 300 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. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.

Sample detector distance = UNKNOWN

3C-like proteinase from SARS-CoV-2 replicase polyprotein 1a, PT9 mutant (MPro PT9)
Mol. type   Protein
Organism   Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2)
Olig. state   Monomer
Mon. MW   33.8 kDa
Sequence   FASTA