8UND

X-ray Structure of SARS-CoV-2 main protease covalently bound to inhibitor GRL-190-21 at 1.90 A.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2022-10-01
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 21 21 2
Unit cell lengths	45.848, 63.968, 105.240
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.080 - 1.900
R-factor	0.1531
Rwork	0.150
R-free	0.20250
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.013
RMSD bond angle	1.196
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHENIX
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.080	1.968
High resolution limit [Å]	1.900	1.900
Rmerge	0.117	0.813
Rmeas	0.124	0.857
Rpim	0.039	0.270
Number of reflections	25135	2459
<I/σ(I)>	17.42	3.18
Completeness [%]	99.8	99.43
Redundancy	9.5	9.3
CC(1/2)	0.999	0.852

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	279	Briefly, 1 uL of ~110 uM SARS-CoV-2 3CLpro in 25 mM HEPES pH 7.5, 2.5 mM DTT containing ~150 uM GRL-190-21 was mixed with 2 uL of reservoir solution which contained a constant concentration of 3 mM DTT, 50 mM MES pH 6.0, 1% MPD, and varying concentrations of PEG-10,000 and KCl.