6N4N
Crystal structure of the designed protein DNCR2/danoprevir/NS3a complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.1 |
| Synchrotron site | ALS |
| Beamline | 8.2.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-06-16 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 70.840, 69.256, 99.344 |
| Unit cell angles | 90.00, 108.59, 90.00 |
Refinement procedure
| Resolution | 94.160 - 2.290 |
| R-factor | 0.2053 |
| Rwork | 0.203 |
| R-free | 0.24080 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3m5l |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.461 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 94.160 | 2.370 |
| High resolution limit [Å] | 2.290 | 2.300 |
| Rmerge | 0.102 | 0.340 |
| Number of reflections | 38559 | 3179 |
| <I/σ(I)> | 14.4 | |
| Completeness [%] | 99.3 | |
| Redundancy | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 295 | 100 mM Bis-Tris, pH 6.5, 200 mM lithium sulfate, 22% PEG3350 |
