5LAK
Ligand-bound structure of Cavally Virus 3CL Protease
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-11-26 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.979742 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 72.192, 110.150, 98.496 |
| Unit cell angles | 90.00, 105.90, 90.00 |
Refinement procedure
| Resolution | 45.333 - 2.299 |
| R-factor | 0.2089 |
| Rwork | 0.208 |
| R-free | 0.22960 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5lac |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.888 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.440 |
| High resolution limit [Å] | 2.299 | 2.299 |
| Rmerge | 0.049 | |
| Number of reflections | 65479 | |
| <I/σ(I)> | 13 | 2.6 |
| Completeness [%] | 99.2 | 98.3 |
| Redundancy | 3.2 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | 0.1M bicine, 20% PEG6000 |
