4RSP
X-ray structure of MERS-CoV nsp5 protease bound with a designed inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-02-13 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 0.9793 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 106.490, 57.312, 48.879 |
| Unit cell angles | 90.00, 112.78, 90.00 |
Refinement procedure
| Resolution | 19.350 - 1.620 |
| R-factor | 0.1643 |
| Rwork | 0.162 |
| R-free | 0.20270 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3v3m |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.274 |
| Data reduction software | MOSFLM |
| Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.350 | 19.350 |
| High resolution limit [Å] | 1.620 | 1.620 |
| Number of reflections | 32843 | |
| <I/σ(I)> | 5.2 | |
| Completeness [%] | 95.0 | 95 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 273 | 0.2 M sodium acetate, 0.1 M Bis-Tris pH-7.0, 20% PEG-3350, VAPOR DIFFUSION, HANGING DROP, temperature 273K |
