M protease SARS CoV-2 with JL-352

Raja Tripathi.

SASDXY6 – M protease of SARS CoV-2 with JL-352 compound

3 Chymotrypsin Like Protease
MWexperimental 74 kDa
MWexpected 68 kDa
VPorod 271 nm3
log I(s) 5.57×104 5.57×103 5.57×102 5.57×101
3 Chymotrypsin Like Protease small angle scattering data  s, nm-1
ln I(s)
3 Chymotrypsin Like Protease Guinier plot ln 5.58×104 Rg: 4.7 nm 0 (4.7 nm)-2 s2
(sRg)2I(s)/I(0)
3 Chymotrypsin Like Protease Kratky plot 1.104 0 √3 sRg
p(r)
3 Chymotrypsin Like Protease pair distance distribution function Rg: 4.3 nm 0 Dmax: 12.3 nm

Data validation

There are no models related to this curve.

SAXS data from solutions of M protease of SARS CoV-2 with JL-352 compound in 50mM Tris, 200mM NaCl, pH 8 were collected on the Anton Paar SAXSpace instrument (CSIR-Central Drug Research Institute, Lucknow, India) using a Mythen2 R 1K detector at a sample-detector distance of 0.3 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 5.00 mg/ml was measured at 10°C. Two successive 1800 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.

M protease of SARS-CoV-2 was purified using Ni-NTA affinity columns, and further purification was done using Size Exclusion Chromatography. The purified protein was then incubated with JL-352 for 30 minutes before SAXS analysis.

3 Chymotrypsin Like Protease (3CL pro)
Mol. type   Protein
Organism   Severe acute respiratory syndrome coronavirus 2
Olig. state   Dimer
Mon. MW   33.8 kDa
 
UniProt   P0DTC1 (3264-3569)
Sequence   FASTA