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 |