7MME

Crystal structure of HCV NS3/4A D168A protease in complex with JZ01-15

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	PIXEL
Collection date	2019-03-20
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.918, 1.13
Spacegroup name	P 21 21 21
Unit cell lengths	55.616, 58.511, 59.938
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	26.380 - 1.560
R-factor	0.1567
Rwork	0.155
R-free	0.18100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5voj
RMSD bond length	0.010
RMSD bond angle	1.502
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]	26.380	1.616
High resolution limit [Å]	1.560	1.560
Number of reflections	28047	2399
<I/σ(I)>	25.2
Completeness [%]	98.3
Redundancy	8.9

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