8H5F

Crystal Structure of SARS-CoV-2 Main Protease (Mpro) L167F Mutant in Complex with Inhibitor Nirmatrelvir

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I04
Synchrotron site	Diamond
Beamline	I04
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-08-10
Detector	DECTRIS EIGER2 X 16M
Wavelength(s)	0.953740
Spacegroup name	P 21 21 2
Unit cell lengths	45.373, 63.825, 105.839
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	27.330 - 1.790
R-factor	0.1869
Rwork	0.184
R-free	0.22730
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7vh8
RMSD bond length	0.008
RMSD bond angle	1.046
Data reduction software	autoPROC
Data scaling software	XSCALE
Phasing software	PHENIX
Refinement software	PHENIX (1.19.2_4158)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	27.330	27.330	1.900
High resolution limit [Å]	1.790	5.280	1.790
Rmerge	0.080	0.033	0.658
Rmeas	0.083	0.035	0.684
Number of reflections	29844	1288	4729
<I/σ(I)>	21.05
Completeness [%]	99.9
Redundancy	13.3
CC(1/2)	1.000	0.999	0.919

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION		293	0.2% w/v Lidocaine hydrochloride monohydrate, 0.2% w/v Procaine hydrochloride, 0.2% w/v Proparacaine hydrochloride, 0.2% w/v tetracaine hydrochloride, 0.1 M Buffer System 3 pH 8.5 (Tris base, BICINE), 20% v/v ethylene glycol, 10% w/v PEG 8,000