3PRP
Structural analysis of a viral OTU domain protease from the Crimean-Congo Hemorrhagic Fever virus in complex with human ubiquitin
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 | 2010-08-23 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.978 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 79.316, 105.845, 113.032 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 77.260 - 1.699 |
| R-factor | 0.174 |
| Rwork | 0.172 |
| R-free | 0.21200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3prm |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.351 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.1.4) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 77.260 | 1.760 |
| High resolution limit [Å] | 1.699 | 1.699 |
| Rmerge | 0.055 | 0.186 |
| Number of reflections | 50853 | |
| <I/σ(I)> | 2.8 | |
| Completeness [%] | 96.5 | 74.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 22-28% PEG 8000, 100 mM Na cacodylate pH 6.5, 100-250 mM Mg acetate, and 2% n-Octyl- -D-glucoside, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
