4YPL
Crystal structure of a hexameric LonA protease bound to three ADPs
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 200 |
| Detector technology | CCD |
| Collection date | 2014-11-22 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 169.044, 169.128, 135.361 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 3.450 |
| R-factor | 0.23859 |
| Rwork | 0.237 |
| R-free | 0.26480 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ypn 1QZM and 1RR9 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.517 |
| Data scaling software | HKL-2000 |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.470 |
| High resolution limit [Å] | 3.450 | 3.450 |
| Number of reflections | 45968 | |
| <I/σ(I)> | 0.168 | 2.53 |
| Completeness [%] | 99.5 | 99.6 |
| Redundancy | 5.6 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 8.7 | 295 | 0.1 M Tris-HCl pH 8.7, 0.1 M CaCl2, 10-13% PEG 3350 |






