3SU1
Crystal structure of NS3/4A protease variant D168A in complex with danoprevir
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-03-09 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 55.018, 58.518, 60.018 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.900 - 1.399 |
| R-factor | 0.1579 |
| Rwork | 0.157 |
| R-free | 0.17800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3M5M CHAIN B |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.371 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.450 |
| High resolution limit [Å] | 1.399 | 3.020 | 1.399 |
| Rmerge | 0.067 | 0.030 | 0.491 |
| Number of reflections | 38857 | ||
| <I/σ(I)> | 9.8 | ||
| Completeness [%] | 100.0 | 99.7 | 100 |
| Redundancy | 6 | 5.8 | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | hanging drop, vapor diffusion | 6.2 | 295 | 20-25% PEG 3350, 0.1M MES (pH 6.5), 4% ammonium sulfate, hanging drop, vapor diffusion, temperature 295K |
