7L7O

Crystal structure of HCV NS3/4A D168A protease in complex with NR04-49

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	CCD
Collection date	2020-10-08
Detector	RIGAKU SATURN 944
Wavelength(s)	1.54178
Spacegroup name	P 21 21 21
Unit cell lengths	55.133, 58.752, 59.731
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.943 - 1.720
R-factor	0.1514
Rwork	0.150
R-free	0.17020
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5voj
RMSD bond length	0.011
RMSD bond angle	1.634
Data reduction software	HKL-3000
Data scaling software	HKL-3000 (703x)
Refinement software	PHENIX (1.12-2829)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.943	1.782
High resolution limit [Å]	1.720	1.720
Number of reflections	21030	5555
<I/σ(I)>	18.43
Completeness [%]	99.1
Redundancy	5.8
CC(1/2)	0.998	0.908

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	298	100 mM MES Buffer pH 6.5, 4% (W/V) Ammonium Sulfate, 20-26% PEG 3350 The crystals were then soaked overnight in cryogenic conditions containing inhibitor (100 mM MES Buffer pH 6.5, 4% (W/V) Ammonium Sulfate, 20-26% PEG 3350, 15% Ethylene glycol, and 10-20 mM of inhibitor in DMF)