1RL2
RIBOSOMAL PROTEIN L2 RNA-BINDING DOMAIN FROM BACILLUS STEAROTHERMOPHILUS
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-18B |
| Synchrotron site | Photon Factory |
| Beamline | BL-18B |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-05-15 |
| Detector | RIGAKU |
| Wavelength(s) | 0.9000, 0.9785, 0.9788 |
| Spacegroup name | P 1 |
| Unit cell lengths | 28.050, 36.190, 69.710 |
| Unit cell angles | 99.58, 95.86, 102.63 |
Refinement procedure
| Resolution | 20.000 - 2.300 |
| R-factor | 0.203 * |
| Rwork | 0.203 |
| R-free | 0.25800 |
| Structure solution method | MAD |
| RMSD bond length | 0.011 |
| RMSD bond angle | 26.100 * |
| Data reduction software | DENZO |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | SHARP |
| Refinement software | CNS (0.5) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.420 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.084 | 0.354 |
| Total number of observations | 45101 * | |
| Number of reflections | 11430 | |
| <I/σ(I)> | 8.3 | 2.1 |
| Completeness [%] | 98.6 | 96.8 |
| Redundancy | 3.9 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.5 | 18 * | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents
| ID | crystal ID | solution ID | reagent name | concentration | details |
| 1 | 1 | 1 | PEK20000 | ||
| 2 | 1 | 1 | MES |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10-15 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | dithiothreitol | 1 (mM) | |
| 4 | 1 | reservoir | PEG20000 | 10-15 (%(w/w)) | |
| 5 | 1 | reservoir | MES | 0.1 (M) |
