7MMA
Crystal structure of HCV NS3/4A 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 | 2019-11-25 |
Detector | RIGAKU SATURN 944 |
Wavelength(s) | 1.54178 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.083, 58.504, 59.688 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 27.040 - 1.650 |
R-factor | 0.1458 |
Rwork | 0.144 |
R-free | 0.18090 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5voj |
RMSD bond length | 0.013 |
RMSD bond angle | 1.559 |
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] | 27.040 | 1.709 |
High resolution limit [Å] | 1.650 | 1.650 |
Number of reflections | 21861 | 1873 |
<I/σ(I)> | 25.34 | |
Completeness [%] | 93.3 | |
Redundancy | 5.3 | |
CC(1/2) | 0.997 | 0.984 |
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 |