1Y2Q
Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-06-06 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 61.752, 61.752, 64.894 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 25.000 - 1.950 |
R-factor | 0.20865 |
Rwork | 0.205 |
R-free | 0.27224 |
Structure solution method | MIR |
RMSD bond length | 0.011 |
RMSD bond angle | 1.324 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.020 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.041 | 0.314 |
Number of reflections | 10459 | |
<I/σ(I)> | 25.3 | 2.25 |
Completeness [%] | 96.7 | 87.2 |
Redundancy | 3.3 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | PEG 8000, Hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K |