3AW1
Structure of SARS 3CL protease auto-proteolysis resistant mutant in the absent of inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-5A |
| Synchrotron site | Photon Factory |
| Beamline | BL-5A |
| Temperature [K] | 95 |
| Detector technology | CCD |
| Collection date | 2009-03-15 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 1 |
| Unit cell lengths | 52.130, 67.454, 67.384 |
| Unit cell angles | 71.23, 77.46, 81.74 |
Refinement procedure
| Resolution | 29.950 - 2.000 |
| R-factor | 0.22572 |
| Rwork | 0.224 |
| R-free | 0.26266 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2zu5 |
| RMSD bond length | 0.023 |
| RMSD bond angle | 2.007 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.030 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.038 | 0.175 |
| Number of reflections | 55659 | |
| <I/σ(I)> | 24.3 | 6.1 |
| Completeness [%] | 97.2 | 95.8 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 277 | 9-11%(w/v) PEG20000, 100mM MES pH 6.0, 5mM DTT , VAPOR DIFFUSION, HANGING DROP, temperature 277K |
