1ASZ
THE ACTIVE SITE OF YEAST ASPARTYL-TRNA SYNTHETASE: STRUCTURAL AND FUNCTIONAL ASPECTS OF THE AMINOACYLATION REACTION
Experimental procedure
| Detector technology | IMAGE PLATE |
| Collection date | 1992-01-01 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 211.270, 145.350, 86.190 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 7.000 - 3.000 |
| R-factor | 0.203 |
| Rwork | 0.203 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 2.300 |
| Data reduction software | MOSFLM |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 3.000 * |
| Rmerge | 0.088 |
| Total number of observations | 135407 * |
| Number of reflections | 46698 |
| Completeness [%] | 87.0 |
| Redundancy | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | 4 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | Tris-maleate/NaOH | 40 (mM) | |
| 2 | 1 | drop | 5 (mM) | ||
| 3 | 1 | drop | ammonium sulfate | 25 (%(w/v)) | |
| 4 | 1 | drop | aspartyl-tRNA synthetase | 10 (mg/ml) | |
| 5 | 1 | reservoir | ammonium sulfate | 60 (%(w/v)) | |
| 6 | 1 | drop | tRNAAsp | 4.8 (mg/ml) |
