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) |