7L7N
Crystal structure of HCV NS3/4A D168A protease in complex with NR02-59
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2020-09-23 |
Detector | RIGAKU SATURN 944 |
Wavelength(s) | 1.54178 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.623, 58.728, 60.209 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 24.050 - 1.590 |
R-factor | 0.1834 |
Rwork | 0.182 |
R-free | 0.20930 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5voj |
RMSD bond length | 0.007 |
RMSD bond angle | 1.168 |
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] | 24.055 | 1.647 |
High resolution limit [Å] | 1.590 | 1.590 |
Number of reflections | 26388 | 2355 |
<I/σ(I)> | 12.48 | |
Completeness [%] | 98.5 | |
Redundancy | 4.6 | |
CC(1/2) | 0.996 | 0.838 |
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 10-20 mM of inhibitor in DMF) |