7L7O
Crystal structure of HCV NS3/4A D168A protease in complex with NR04-49
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2020-10-08 |
Detector | RIGAKU SATURN 944 |
Wavelength(s) | 1.54178 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 55.133, 58.752, 59.731 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.943 - 1.720 |
R-factor | 0.1514 |
Rwork | 0.150 |
R-free | 0.17020 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5voj |
RMSD bond length | 0.011 |
RMSD bond angle | 1.634 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 (703x) |
Refinement software | PHENIX (1.12-2829) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.943 | 1.782 |
High resolution limit [Å] | 1.720 | 1.720 |
Number of reflections | 21030 | 5555 |
<I/σ(I)> | 18.43 | |
Completeness [%] | 99.1 | |
Redundancy | 5.8 | |
CC(1/2) | 0.998 | 0.908 |
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) |