7MM3

Crystal structure of HCV NS3/4A protease in complex with NR01-127

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	CCD
Collection date	2019-06-05
Detector	RIGAKU SATURN 944
Wavelength(s)	1.54178
Spacegroup name	P 21 21 21
Unit cell lengths	54.882, 58.653, 59.857
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	22.950 - 1.780
R-factor	0.1525
Rwork	0.150
R-free	0.18950
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5voj
RMSD bond length	0.012
RMSD bond angle	1.388
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]	22.950	1.884
High resolution limit [Å]	1.780	1.780
Number of reflections	18600	1679
<I/σ(I)>	18.57
Completeness [%]	97.4
Redundancy	6.3
CC(1/2)	0.998	0.939

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		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