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 |