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 |