2BO1
Crystal structure of a hybrid ribosomal protein L30e with surface residues from T. celer, and core residues from yeast
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 6B |
| Synchrotron site | PAL/PLS |
| Beamline | 6B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | BRUKER |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 29.187, 52.531, 52.692 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 37.190 - 1.700 |
| R-factor | 0.176 |
| Rwork | 0.173 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1h7m |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.305 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | REFMAC (5.2.0003) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.060 | 0.090 |
| Number of reflections | 9277 | |
| <I/σ(I)> | 63 | 34 |
| Completeness [%] | 98.6 | 94.9 |
| Redundancy | 5.6 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 2UL 10MG/ML PROTEIN AND 2UL 22.5% PEG3350, 0.1M TRIS PH 8.5, CRYOPROTECTED IN 20% PEG 400 |
