4RRL
E129A mutant of N-terminal editing domain of threonyl-tRNA synthetase from Aeropyrum pernix with L-Ser3AA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2012-05-23 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.5418 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 47.023, 47.023, 112.514 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 24.890 - 1.965 |
R-factor | 0.18716 |
Rwork | 0.185 |
R-free | 0.23579 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.016 |
RMSD bond angle | 1.656 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.7.0025) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 25.000 |
High resolution limit [Å] | 1.960 |
Number of reflections | 8950 |
Completeness [%] | 97.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 277 | 0.1M Tris HCl pH 8.5, 0.2M MgCl2, 30% PEG4000, VAPOR DIFFUSION, HANGING DROP, temperature 277K |