1DD5
CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA RIBOSOME RECYCLING FACTOR, RRF
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-03-27 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9786,0.9788,0.9184 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 47.250, 47.250, 297.550 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.550 |
| R-factor | 0.232 |
| Rwork | 0.230 |
| R-free | 0.27700 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 22.300 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MLPHARE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.650 |
| High resolution limit [Å] | 2.550 | 2.550 |
| Rmerge | 0.049 | 0.153 |
| Number of reflections | 11648 | |
| <I/σ(I)> | 27 | 9.5 |
| Completeness [%] | 97.4 | 91.8 |
| Redundancy | 6.7 | 5.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.6 * | 298 | drop consists of equal volume of protein and reservoir solutions * |
| 1 | Vapor diffusion, hanging drop * | 7.6 * | 298 | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | 50 (mM) | ||
| 4 | 1 | drop | dithiothreitol | 0.5 (mM) | |
| 5 | 1 | reservoir | sodium acetate | 0.1 (M) | |
| 6 | 1 | reservoir | ammonium sulfate | 2.0 (M) |
