1EQR
CRYSTAL STRUCTURE OF FREE ASPARTYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | LURE BEAMLINE DW32 |
| Synchrotron site | LURE |
| Beamline | DW32 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-03-27 |
| Detector | MARRESEARCH |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 117.749, 161.958, 131.599 |
| Unit cell angles | 90.00, 110.36, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.700 |
| R-factor | 0.197 * |
| Rwork | 0.198 |
| R-free | 0.26900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | E.coli aspartyl-tRNA synthetase - S. cerevisiae tRNA(Asp) complex (Moulinier unpublished) |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.600 |
| Data reduction software | DENZO |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.790 |
| High resolution limit [Å] | 2.650 | 2.650 |
| Rmerge | 0.048 | 0.178 |
| Number of reflections | 60472 * | 8888 * |
| <I/σ(I)> | 10.3 | 2.7 |
| Completeness [%] | 90.2 | 92.3 |
| Redundancy | 1.76 | 1.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 288 * | Boeglin, M., (1996) Acta Crystallog. sect., D52, 211. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | drop | PEG6000 | 5.0 (%) | |
| 3 | 1 | drop | 530 (mM) | ||
| 4 | 1 | drop | Bis-Tris | 33 (mM) | |
| 5 | 1 | reservoir | Bis-Tris | 100 (mM) | |
| 6 | 1 | reservoir | PEG6000 | 16 (%) | |
| 7 | 1 | reservoir | 1.6 (M) |
