2HL1
Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with seryl-3'-aminoadenosine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-08-05 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 40.991, 75.735, 95.294 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.400 - 2.250 |
| R-factor | 0.205 |
| Rwork | 0.205 |
| R-free | 0.28800 |
| 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 | 2.330 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.061 | 0.301 |
| Number of reflections | 13321 | |
| <I/σ(I)> | 15.82 | 2.7 |
| Completeness [%] | 90.7 | 83.9 |
| Redundancy | 3.6 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | 25% PEG 3350, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
