2X36
Structure of the proteolytic domain of the Human Mitochondrial Lon protease
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-08-30 |
| Detector | ADSC CCD |
| Wavelength(s) | 0.9395, 0.9395 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 69.800, 83.750, 105.490 |
| Unit cell angles | 90.00, 90.05, 90.00 |
Refinement procedure
| Resolution | 34.000 - 2.000 |
| R-factor | 0.19549 |
| Rwork | 0.194 |
| R-free | 0.23230 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1rre |
| RMSD bond length | 0.027 |
| RMSD bond angle | 2.095 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 2.110 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.060 | 0.730 |
| Number of reflections | 82419 | |
| <I/σ(I)> | 10.9 | 1.7 |
| Completeness [%] | 99.4 | 99.9 |
| Redundancy | 3.6 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 0.1 M BIS-TRIS PROPANOL PH 6.5, 0.25 M SODIUM ACETATE, 28% PEG 3350 |
