3SU4
Crystal structure of NS3/4A protease variant R155K in complex with vaniprevir
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 |
| Collection date | 2010-12-07 |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 61 |
| Unit cell lengths | 85.762, 85.762, 97.414 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 42.880 - 2.255 |
| R-factor | 0.1695 |
| Rwork | 0.167 |
| R-free | 0.22330 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.263 |
| 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 | 2.330 |
| High resolution limit [Å] | 2.250 | 4.850 | 2.250 |
| Rmerge | 0.103 | 0.045 | 0.436 |
| Number of reflections | 19213 | ||
| <I/σ(I)> | 7.2 | ||
| Completeness [%] | 99.9 | 99 | 100 |
| Redundancy | 7.9 | 7.8 | 7.9 |
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 |
