6C2M
Crystal structure of HCV NS3/4A protease variant Y56H in complex with MK-5172
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-07-07 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 56.635, 103.326, 73.962 |
Unit cell angles | 90.00, 112.01, 90.00 |
Refinement procedure
Resolution | 35.725 - 1.859 |
R-factor | 0.1842 |
Rwork | 0.180 |
R-free | 0.22420 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5voj |
RMSD bond length | 0.005 |
RMSD bond angle | 0.888 |
Data scaling software | HKL-3000 (703x) |
Phasing software | PHASER |
Refinement software | PHENIX ((1.12_2829: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.725 | 1.906 |
High resolution limit [Å] | 1.859 | 1.859 |
Number of reflections | 63506 | |
<I/σ(I)> | 11.4 | |
Completeness [%] | 96.0 | |
Redundancy | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 100 mM MES BUFFER PH 6.5, 4% (W/V) AMMONIUM SULFATE, 20-26% PEG 3350 |