4HI3
Crystal structure of dimeric R298A mutant of SARS coronavirus main protease
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-03-08 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.976 |
| Spacegroup name | P 1 |
| Unit cell lengths | 55.042, 59.444, 59.822 |
| Unit cell angles | 71.29, 73.40, 72.31 |
Refinement procedure
| Resolution | 30.000 - 2.090 |
| R-factor | 0.19241 |
| Rwork | 0.190 |
| R-free | 0.24138 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1uk4 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.330 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.160 |
| High resolution limit [Å] | 2.090 | 2.090 |
| Number of reflections | 35837 | |
| Completeness [%] | 94.7 | 94.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 295 | 30% PEG 300, 5% PEG 1000, 0.1 M Tris, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
