7MML

Crystal structure of HCV NS3/4A D168A protease in complex with NR01-145

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	CCD
Collection date	2019-11-02
Detector	RIGAKU SATURN 944
Wavelength(s)	1.54178
Spacegroup name	P 21 21 21
Unit cell lengths	54.037, 58.592, 59.565
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	27.020 - 1.701
R-factor	0.1616
Rwork	0.160
R-free	0.19430
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5voj
RMSD bond length	0.018
RMSD bond angle	1.966
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]	27.020	1.762
High resolution limit [Å]	1.701	1.701
Rmerge		0.311
Number of reflections	21349	2063
<I/σ(I)>	19.69
Completeness [%]	99.8
Redundancy	5.1
CC(1/2)	0.999	0.904

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