7AWS

Structure of SARS-CoV-2 Main Protease bound to TH-302.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PETRA III, DESY BEAMLINE P11
Synchrotron site	PETRA III, DESY
Beamline	P11
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-04-06
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	1.0332
Spacegroup name	C 1 2 1
Unit cell lengths	113.050, 53.039, 44.782
Unit cell angles	90.00, 102.75, 90.00

Refinement procedure

Resolution	55.130 - 1.810
R-factor	0.2032
Rwork	0.201
R-free	0.23850
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6y2e
RMSD bond length	0.003
RMSD bond angle	0.646
Data reduction software	DIALS (1.8.5)
Data scaling software	DIALS (1.8.5)
Phasing software	PHASER
Refinement software	PHENIX (1.18-3855_9999)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	55.170	1.860
High resolution limit [Å]	1.810	1.810
Rmerge	0.120	0.683
Rmeas	0.142	0.803
Rpim	0.074	0.417
Number of reflections	23780	1756
<I/σ(I)>	5	1.2
Completeness [%]	100.0	100
Redundancy	3.5	3.6
CC(1/2)	0.992	0.599

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	291	Co-crystallization with the compounds was achieved by equlibrating a 6.25 mg/ml protein solution in 20 mM HEPES buffer (pH 7.8) containing 1 mM DTT, 1mM EDTA, and 150 mM NaCl against a reservoir solution of 100 mM MIB buffer (2:3:3 molar ratio of malonic acid, imidazole, and boric acid), pH 7.5, containing 25% v/v PEG 1500 and 5% v/v DMSO. Prior to crystallization compound solutions in DMSO were dried onto the wells of SwissCI 96-well plates. To achieve reproducible crystal growth seeding was used. Crystals appeared within a few hours and reached their final size after 2 -3 days.