3AVZ
Structure of SARS 3CL protease with peptidic aldehyde inhibitor containing cyclohexyl side chain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-6A |
| Synchrotron site | Photon Factory |
| Beamline | BL-6A |
| Temperature [K] | 95 |
| Detector technology | CCD |
| Collection date | 2010-01-27 |
| Detector | ADSC QUANTUM 4r |
| Wavelength(s) | 0.978 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 109.185, 80.533, 52.987 |
| Unit cell angles | 90.00, 105.05, 90.00 |
Refinement procedure
| Resolution | 43.450 - 2.460 |
| R-factor | 0.22351 |
| Rwork | 0.221 |
| R-free | 0.26261 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2zu5 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.781 |
| 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] | 50.000 | 2.540 |
| High resolution limit [Å] | 2.460 | 2.500 |
| Rmerge | 0.122 | 0.487 |
| Number of reflections | 15377 | |
| <I/σ(I)> | 16.736 | 2.526 |
| Completeness [%] | 97.4 | 83.2 |
| Redundancy | 7.4 | 5.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 277 | 9-11%(w/v) PEG 20000, 100mM MES pH 6.0, 5mM DTT , VAPOR DIFFUSION, HANGING DROP, temperature 277K |
