5E7S
Hexameric structure of a LonA protease domain in active state
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL15A1 |
| Synchrotron site | NSRRC |
| Beamline | BL15A1 |
| Temperature [K] | 200 |
| Detector technology | CCD |
| Collection date | 2014-06-19 |
| Detector | RAYONIX MX-325 |
| Wavelength(s) | 0.8 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 116.309, 212.787, 178.921 |
| Unit cell angles | 90.00, 100.80, 90.00 |
Refinement procedure
| Resolution | 20.000 - 3.030 |
| R-factor | 0.23 |
| Rwork | 0.227 |
| R-free | 0.27900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ypm |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.947 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 175.800 | 3.160 |
| High resolution limit [Å] | 3.030 | 3.050 |
| Rmerge | 0.700 | |
| Number of reflections | 74605 | |
| <I/σ(I)> | 16.7 | 2.33 |
| Completeness [%] | 90.9 | 93.8 |
| Redundancy | 4.7 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 6.5 | 295 | 0.2M sodium citrate pH6.5, 12% PEG 3350 |
