3SU2
Crystal structure of NS3/4A protease variant A156T 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 | 2010-12-07 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.885, 58.528, 59.970 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.490 - 1.496 |
| R-factor | 0.1551 |
| Rwork | 0.154 |
| R-free | 0.17720 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3M5M CHAIN B |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.399 |
| 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 | 1.550 |
| High resolution limit [Å] | 1.496 | 3.230 | 1.496 |
| Rmerge | 0.065 | 0.027 | 0.502 |
| Number of reflections | 31822 | ||
| <I/σ(I)> | 10 | ||
| Completeness [%] | 100.0 | 99.8 | 100 |
| Redundancy | 7.2 | 6.9 | 7.1 |
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 |
