7UVN
Crystal structure of human ClpP protease in complex with TR-57
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) | 0.98 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 142.098, 153.040, 104.696 |
Unit cell angles | 90.00, 117.92, 90.00 |
Refinement procedure
Resolution | 49.250 - 3.110 |
R-factor | 0.232 |
Rwork | 0.229 |
R-free | 0.28300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6bba |
Data reduction software | MOSFLM |
Data scaling software | Aimless |
Phasing software | PHENIX |
Refinement software | PHENIX (1.20) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 3.150 |
High resolution limit [Å] | 3.100 | 8.400 | 3.100 |
Rmerge | 0.285 | 0.103 | 1.065 |
Rmeas | 0.307 | 0.111 | 1.146 |
Rpim | 0.113 | 0.041 | 0.419 |
Total number of observations | 253214 | ||
Number of reflections | 35316 | 1818 | 1762 |
<I/σ(I)> | 2.6 | ||
Completeness [%] | 99.7 | 99.9 | 99.4 |
Redundancy | 7.2 | 7.1 | 7.3 |
CC(1/2) | 0.996 | 0.705 |
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 |