8P56

Crystal structure of the main protease (3CLpro/Mpro) of SARS-CoV-2 obtained in presence of 150 micromolar X77.

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	67.941, 101.009, 104.201
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.450 - 1.630
R-factor	0.1636
Rwork	0.163
R-free	0.18400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7bb2
RMSD bond length	0.008
RMSD bond angle	0.977
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]	104.200	1.660
High resolution limit [Å]	1.630	1.630
Rmerge	0.084
Number of reflections	90072	4422
<I/σ(I)>	14
Completeness [%]	100.0
Redundancy	9
CC(1/2)	0.999	0.613

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, 0.1M Hepes/MOPS pH 7.5, 20% v/v Ethylene glycol 10 % w/v PEG 8000