7L7P

Crystal structure of HCV NS3/4A D168A protease in complex with CH-24

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	CCD
Collection date	2020-10-05
Detector	RIGAKU SATURN 944
Wavelength(s)	1.54178
Spacegroup name	P 21 21 21
Unit cell lengths	55.062, 60.042, 58.808
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.934 - 1.580
R-factor	0.1638
Rwork	0.163
R-free	0.18450
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5voj
RMSD bond length	0.013
RMSD bond angle	1.442
Data reduction software	HKL-3000
Data scaling software	HKL-3000 (703x)
Phasing software	PHASER
Refinement software	PHENIX (1.12-2829)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	24.934	1.637
High resolution limit [Å]	1.580	1.580
Number of reflections	26628	2356
<I/σ(I)>	23.46
Completeness [%]	97.2
Redundancy	4.7
CC(1/2)	0.998	0.965

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 or 20 mM of inhibitor in DMF)