1IQ4
5S-RRNA BINDING RIBOSOMAL PROTEIN L5 FROM BACILLUS STEAROTHERMOPHILUS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL44B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-12-08 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.7 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 138.650, 49.220, 68.930 |
| Unit cell angles | 90.00, 117.32, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.800 |
| R-factor | 0.215 * |
| Rwork | 0.215 |
| R-free | 0.25910 |
| Structure solution method | MAD and MR |
| RMSD bond length | 0.045 |
| RMSD bond angle | 21.880 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | SHARP |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.050 | 0.239 * |
| Total number of observations | 252800 * | |
| Number of reflections | 37507 | |
| <I/σ(I)> | 7.6 | 3.7 |
| Completeness [%] | 97.7 | 96.6 |
| Redundancy | 6.7 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 18 * | PEG8000, HEPES, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | HEPES | 0.1 (M) | |
| 3 | 1 | reservoir | PEG8000 | 16 (%) | |
| 4 | 1 | reservoir | MPD | 10 (%) |
