7UVR
Crystal structure of human ClpP protease in complex with TR-65
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08B1-1 |
| Synchrotron site | CLSI |
| Beamline | 08B1-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-08-03 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.9201 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 142.171, 152.515, 104.268 |
| Unit cell angles | 90.00, 118.10, 90.00 |
Refinement procedure
| Resolution | 29.350 - 2.860 |
| R-factor | 0.2052 |
| Rwork | 0.203 |
| R-free | 0.25260 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6bba |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.350 | 2.930 |
| High resolution limit [Å] | 2.860 | 2.860 |
| Rmerge | 0.207 | |
| Number of reflections | 44929 | 44929 |
| <I/σ(I)> | 6 | |
| Completeness [%] | 99.2 | |
| Redundancy | 5.2 | |
| CC(1/2) | 0.987 | 0.628 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 294 | 0.1 M sodium acetate pH 4.6 to 5.2, 5% PEG 4000 |






