2VJ1
A Structural View of the Inactivation of the SARS-Coronavirus Main Proteinase by Benzotriazole Esters
Replaces: 2CGGExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-11-07 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 52.231, 97.760, 67.709 |
| Unit cell angles | 90.00, 103.01, 90.00 |
Refinement procedure
| Resolution | 65.940 - 2.250 |
| R-factor | 0.187 |
| Rwork | 0.183 |
| R-free | 0.25600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1uj1 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.574 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.3.0037) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.270 | 2.340 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.070 | 0.470 |
| Number of reflections | 31422 | |
| <I/σ(I)> | 12.9 | 1.91 |
| Completeness [%] | 99.7 | 100 |
| Redundancy | 3.2 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 5% PEG10000, 0.1M MES PH6.5, 3% ETHYLNE GLYCOL, 50MM NH4-ACETATE |
