6NZT
Crystal structure of HCV NS3/4A protease in complex with voxilaprevir
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.1 |
Synchrotron site | ALS |
Beamline | 5.0.1 |
Temperature [K] | 93 |
Detector technology | CCD |
Collection date | 2012-11-01 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.976 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 55.194, 59.009, 60.166 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 33.488 - 1.400 |
R-factor | 0.1768 |
Rwork | 0.176 |
R-free | 0.19690 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3m5l |
RMSD bond length | 0.006 |
RMSD bond angle | 0.900 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX ((1.12_2829: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.440 |
High resolution limit [Å] | 1.400 | 1.400 |
Rmerge | 0.049 | 0.300 |
Number of reflections | 233937 | |
<I/σ(I)> | 36.5 | |
Completeness [%] | 99.2 | |
Redundancy | 6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 8-12% PEG 3350, 0.1M ammonium sulfate, 0.1M MES pH 6.5 |