5N19
Structure of SARS coronavirus main protease in complex with the alpha-ketoamide (S)-N-benzyl-3-((S)-2-cinnamamido-3-phenylpropanamido)-2-oxo-4-((S)-2-oxopyrrolidin-3-yl)butanamide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-12-01 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.0000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 108.196, 82.284, 53.435 |
| Unit cell angles | 90.00, 103.95, 90.00 |
Refinement procedure
| Resolution | 64.770 - 1.620 |
| R-factor | 0.17391 |
| Rwork | 0.172 |
| R-free | 0.20045 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | SARS main protease |
| RMSD bond length | 0.028 |
| RMSD bond angle | 2.484 |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 64.770 | 1.710 |
| High resolution limit [Å] | 1.620 | 1.620 |
| Rmerge | 0.034 | 0.490 |
| Rpim | 0.014 | 0.198 |
| Number of reflections | 56530 | 8106 |
| <I/σ(I)> | 24.5 | 3.4 |
| Completeness [%] | 98.2 | 97.4 |
| Redundancy | 6.8 | 7 |
| CC(1/2) | 1.000 | 0.960 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | 6 - 8% polyethylene glycol 6000, 0.1 M MES, pH 6.0 |
