8AA8
30S ribosomal protein S24e from Thermococcus barophilus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID30B |
| Synchrotron site | ESRF |
| Beamline | ID30B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-04-23 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.96 |
| Spacegroup name | P 1 |
| Unit cell lengths | 24.306, 35.067, 48.897 |
| Unit cell angles | 91.36, 89.95, 92.18 |
Refinement procedure
| Resolution | 48.880 - 1.710 |
| R-factor | 0.18775 |
| Rwork | 0.186 |
| R-free | 0.22514 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7zvm |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.485 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0352) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.880 | 1.830 |
| High resolution limit [Å] | 1.710 | 1.710 |
| Number of reflections | 15519 | 2560 |
| <I/σ(I)> | 1.6 | |
| Completeness [%] | 92.0 | |
| Redundancy | 1.72 | |
| CC(1/2) | 0.936 | 0.255 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 295 | 0,1 M MES pH 6,5, 30 %(v/v) PEG 300 |
