7L7N

Crystal structure of HCV NS3/4A D168A protease in complex with NR02-59

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	CCD
Collection date	2020-09-23
Detector	RIGAKU SATURN 944
Wavelength(s)	1.54178
Spacegroup name	P 21 21 21
Unit cell lengths	54.623, 58.728, 60.209
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.050 - 1.590
R-factor	0.1834
Rwork	0.182
R-free	0.20930
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5voj
RMSD bond length	0.007
RMSD bond angle	1.168
Data reduction software	HKL-3000
Data scaling software	HKL-3000 (703x)
Phasing software	PHASER
Refinement software	PHENIX (1.18.2_3874)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	24.055	1.647
High resolution limit [Å]	1.590	1.590
Number of reflections	26388	2355
<I/σ(I)>	12.48
Completeness [%]	98.5
Redundancy	4.6
CC(1/2)	0.996	0.838

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)