6JI2
Crystal structure of archaeal ribosomal protein aP1, aPelota, and GTP-bound aEF1A complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-5A |
| Synchrotron site | Photon Factory |
| Beamline | BL-5A |
| Temperature [K] | 95 |
| Detector technology | CCD |
| Collection date | 2017-05-12 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 1 |
| Unit cell lengths | 71.447, 73.405, 108.142 |
| Unit cell angles | 98.64, 93.80, 100.44 |
Refinement procedure
| Resolution | 106.420 - 3.000 |
| R-factor | 0.20311 |
| Rwork | 0.199 |
| R-free | 0.27922 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3wxm |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.316 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.8.0124) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 106.420 | 3.050 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.070 | 0.564 |
| Number of reflections | 41897 | |
| <I/σ(I)> | 20.4 | |
| Completeness [%] | 98.9 | |
| Redundancy | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 100 mM Tris-HCl, pH 8.0, 200 mM Li2SO4, 16% (w/v) PEG3350 |
