8P5A

Crystal structure of the main protease (3CLpro/Mpro) of SARS-CoV-2 obtained in presence of 5 millimolar X77 enantiomer R.

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	2021-06-02
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.9718
Spacegroup name	P 21 21 21
Unit cell lengths	67.568, 100.247, 103.919
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.320 - 1.660
R-factor	0.1669
Rwork	0.166
R-free	0.18890
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7bb2
RMSD bond length	0.009
RMSD bond angle	1.153
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]	103.920	1.690
High resolution limit [Å]	1.660	1.660
Rmerge	0.097
Number of reflections	83674	4042
<I/σ(I)>	14
Completeness [%]	99.7
Redundancy	11
CC(1/2)	0.999	0.661

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	0.12 M Diethylene glycol 0.12M Triethylene glycol 0.12M Tetraethylene glycol 0.12M Pentaethylene glycol, 0.1 M Tris/bicine pH 8.5, 20% v/v Ethylene glycol, 10% w/v PEG 8000