5C3N
Crystal structure of MERS coronavirus main protease in spacegroup C2221
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13C1 |
| Synchrotron site | NSRRC |
| Beamline | BL13C1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-05-20 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97622 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 87.230, 94.037, 155.059 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 3.000 |
| R-factor | 0.22128 |
| Rwork | 0.218 |
| R-free | 0.28172 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hi3 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.502 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Refinement software | REFMAC (5.8.0123) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.110 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.170 | 0.629 |
| Number of reflections | 12278 | |
| <I/σ(I)> | 10.2 | 3.1 |
| Completeness [%] | 94.6 | 95.2 |
| Redundancy | 5.5 | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.4 | 295 | 12% PEG 4000, 0.2 M Sodium Acetate, 0.1 M Tris-Cl (pH 8.4) |
