7MMC

Crystal structure of HCV NS3/4A D168A protease in complex with NR01-115

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	CCD
Collection date	2020-02-10
Detector	RIGAKU SATURN 944
Wavelength(s)	1.54178
Spacegroup name	P 21 21 21
Unit cell lengths	45.330, 58.919, 96.208
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.050 - 2.001
R-factor	0.1887
Rwork	0.187
R-free	0.21400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5voj
RMSD bond length	0.003
RMSD bond angle	0.831
Data scaling software	HKL-3000 (703x)
Phasing software	PHASER
Refinement software	PHENIX (1.19.1_4122)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	24.050	2.072
High resolution limit [Å]	2.001	2.001
Number of reflections	17311	1466
<I/σ(I)>	15.25
Completeness [%]	96.0
Redundancy	6
CC(1/2)	0.982	0.975

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 cryogenic condition is 100 mM MES Buffer pH 6.5, 4% (W/V) Ammonium Sulfate, 20-26% PEG 3350, 15% Ethylene glycol