7UVU
Crystal structure of human ClpP protease in complex with TR-107
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 | 2020-08-03 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.98 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 142.147, 152.662, 104.342 |
Unit cell angles | 90.00, 118.01, 90.00 |
Refinement procedure
Resolution | 48.470 - 3.240 |
R-factor | 0.1945 |
Rwork | 0.190 |
R-free | 0.26080 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6bba |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | PHENIX (1.19_4092) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 3.360 |
High resolution limit [Å] | 3.240 | 8.940 | 3.300 |
Rmerge | 0.286 | 0.082 | 0.943 |
Rmeas | 0.310 | 0.088 | 1.028 |
Rpim | 0.119 | 0.033 | 0.405 |
Number of reflections | 30288 | 1575 | 1449 |
<I/σ(I)> | 1.9 | ||
Completeness [%] | 98.7 | 99.8 | 96.6 |
Redundancy | 6.6 | 6.8 | 6.1 |
CC(1/2) | 0.996 | 0.570 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 294 | 0.1 M sodium acetate, 5% PEG 4000 |