2HKZ
Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with L-serine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-08-19 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.5418 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 61.906, 61.906, 64.607 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 24.760 - 2.100 |
R-factor | 0.22 |
Rwork | 0.220 |
R-free | 0.28600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1y2q |
RMSD bond length | 0.006 |
RMSD bond angle | 1.400 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CCP4 ((MOLREP)) |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.070 | 0.388 |
Number of reflections | 8413 | |
<I/σ(I)> | 12.77 | 1.85 |
Completeness [%] | 96.7 | 84.6 |
Redundancy | 2.9 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | 25% PEG 8000, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |