7CRA
Crystal structure of the N-terminal fragment (residue 1-291) of LonA protease from Meiothermus taiwanensis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-1A |
| Synchrotron site | Photon Factory |
| Beamline | BL-1A |
| Temperature [K] | 80 |
| Detector technology | PIXEL |
| Collection date | 2014-02-19 |
| Detector | DECTRIS EIGER2 X 4M |
| Wavelength(s) | 0.95 |
| Spacegroup name | P 63 2 2 |
| Unit cell lengths | 86.016, 86.016, 110.126 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 1.700 |
| R-factor | 0.186 |
| Rwork | 0.184 |
| R-free | 0.22080 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7cr9 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.368 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.069 | 0.779 |
| Number of reflections | 27083 | 2632 |
| <I/σ(I)> | 49.1 | |
| Completeness [%] | 100.0 | |
| Redundancy | 20.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 5.8 | 295 | 0.1 M MES (pH 5.8) and 0.8 M ammonium sulfate |
