1BXE
RIBOSOMAL PROTEIN L22 FROM THERMUS THERMOPHILUS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I711 |
| Synchrotron site | MAX II |
| Beamline | I711 |
| Temperature [K] | 287 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 32.640, 65.930, 67.830 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.900 |
| R-factor | 0.189 |
| Rwork | 0.189 |
| R-free | 0.21900 |
| Structure solution method | MIR |
| RMSD bond length | 0.008 |
| RMSD bond angle | 26.320 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CCP4 |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.053 | 0.159 |
| Number of reflections | 12173 | |
| Completeness [%] | 98.0 | 94.8 |
| Redundancy | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 4.5 * | pH 7 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15 (mg/ml) | |
| 2 | 1 | reservoir | ammonium hydrogen phosphate | 2.0 (M) |






