8P5B

Crystal structure of the main protease (3CLpro/Mpro) of SARS-CoV-2 obtained in presence of 500 micromolar X77 enantiomer S.

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	67.930, 99.831, 103.720
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	51.860 - 1.470
R-factor	0.1651
Rwork	0.164
R-free	0.17800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7bb2
RMSD bond length	0.006
RMSD bond angle	0.933
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]	103.720	1.490
High resolution limit [Å]	1.470	1.470
Rmerge	0.076
Number of reflections	121551	5949
<I/σ(I)>	13.9
Completeness [%]	100.0
Redundancy	8.9
CC(1/2)	0.999	0.664

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	0.1 M Sodium formate 0.1M Ammonium acetate 0.1M Sodium citrate tribasic dihydrate 0.1M Potassium sodium tartrate tetrahydrate 0.1M Sodium oxamate, 0.1M imidazole/MES pH 6.5, 12.5% v/v MPD 12.5% PEG 1000 12.5% w/v PEG 3350