8P54

Crystal structure of the main protease (3CLpro/Mpro) of SARS-CoV-2 obtained in presence of 150 micromolar MG-132.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ELETTRA BEAMLINE 11.2C
Synchrotron site	ELETTRA
Beamline	11.2C
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-05-12
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.9999
Spacegroup name	P 21 21 21
Unit cell lengths	67.742, 99.719, 103.601
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	44.930 - 1.600
R-factor	0.1672
Rwork	0.166
R-free	0.18600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7bb2
RMSD bond length	0.010
RMSD bond angle	0.974
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.19.2_4158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	71.850	1.630
High resolution limit [Å]	1.600	1.600
Rmerge	0.088
Number of reflections	93197	4580
<I/σ(I)>	13.8
Completeness [%]	100.0
Redundancy	8.8
CC(1/2)	0.999	0.618

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	0.12M 1,6-Hexanediol 0.12M 1-Butanol 0.12M 1,2-Propanediol 0.12M 2-Propanol 0.12M 1,4-Butanediol 0.12M 1,3-Propanediol, 0.1 M imidazole/MES pH 6.5, 20% v/v PEG 500 MME 10 % w/v PEG 20000