7L7L

Crystal structure of HCV NS3/4A D168A protease in complex with NR01-129

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	CCD
Collection date	2020-09-15
Detector	RIGAKU SATURN 944
Wavelength(s)	1.54178
Spacegroup name	P 21 21 21
Unit cell lengths	54.856, 58.773, 59.980
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.990 - 1.880
R-factor	0.168
Rwork	0.166
R-free	0.20830
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5voj
RMSD bond length	0.011
RMSD bond angle	1.433
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]	20.990	1.950
High resolution limit [Å]	1.880	1.880
Rmerge	0.095
Number of reflections	15940	1544
<I/σ(I)>	10.02
Completeness [%]	99.5
Redundancy	5.2
CC(1/2)		0.905

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)