9PN7
Crystal structure of human mitochondrial ClpP protease C144R mutant
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 | 2022-11-29 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 142.162, 146.561, 102.046 |
| Unit cell angles | 90.00, 120.17, 90.00 |
Refinement procedure
| Resolution | 44.110 - 3.020 |
| R-factor | 0.2253 |
| Rwork | 0.223 |
| R-free | 0.25630 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.435 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.150 |
| High resolution limit [Å] | 3.020 | 3.100 |
| Rmerge | 0.250 | 2.047 |
| Rmeas | 0.271 | |
| Rpim | 0.103 | |
| Number of reflections | 34157 | 2588 |
| <I/σ(I)> | 5.4 | |
| Completeness [%] | 96.1 | |
| Redundancy | 6.7 | |
| CC(1/2) | 0.988 | 0.391 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 296.15 | 0.1 M sodium acetate trihydrate, pH 4.6 4% w/v polyethylene glycol 4,000 |
