23MA

Crystal structure of SARS-CoV-2 main protease H172Y mutant in complex with leritrelvir

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL19U1
Synchrotron site	SSRF
Beamline	BL19U1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-09-08
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.97923
Spacegroup name	P 1 21 1
Unit cell lengths	48.953, 106.450, 54.036
Unit cell angles	90.00, 102.90, 90.00

Refinement procedure

Resolution	53.225 - 2.267
Rwork	0.170
R-free	0.24020
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.379
Data reduction software	XDS (BUILT 20240630)
Data scaling software	Aimless (0.7.7)
Phasing software	PHASER (2.8.3)
Refinement software	REFMAC (5.8.0430)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	53.225	2.340
High resolution limit [Å]	2.267	2.270
Rmerge	0.121	0.876
Number of reflections	23949	1978
<I/σ(I)>	13.2	2.8
Completeness [%]	95.5
Redundancy	6.4
CC(1/2)	0.997	0.818

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		289	2% v/v TacsimateTM pH 6.0, 0.1 M BIS-TRIS pH 6.5, 20% w/v Polyethylene glycol 3,350