8H51

Crystal Structure of SARS-CoV-2 Main Protease (Mpro) Double Mutant (T21I and E166V) 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	45.566, 63.394, 106.240
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	27.960 - 2.180
R-factor	0.1921
Rwork	0.188
R-free	0.23430
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7vh8
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]	27.960	27.960	2.310
High resolution limit [Å]	2.180	6.370	2.180
Rmerge	0.108	0.037	0.697
Rmeas	0.112	0.039	0.724
Total number of observations	227649
Number of reflections	16779	753	2614
<I/σ(I)>	18	52.35	3.58
Completeness [%]	99.8	98	99.2
Redundancy	13.567	12.153	13.862
CC(1/2)	0.999	0.999	0.891

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 Glycerol, 10% w/v PEG 4,000