1H4Q
Prolyl-tRNA synthetase from Thermus thermophilus complexed with tRNApro(CGG), ATP and prolinol
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID2 |
| Synchrotron site | ESRF |
| Beamline | ID2 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-06-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 141.290, 141.290, 237.560 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 3.000 |
| R-factor | 0.221 |
| Rwork | 0.221 |
| R-free | 0.25400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1HC7 (LIGAND FREE PROLYL-TRNA SYNTHETASE) |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.392 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | CNS (0.4) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 3.080 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.067 | 0.269 |
| Total number of observations | 184299 * | |
| Number of reflections | 48648 | |
| <I/σ(I)> | 2.7 | |
| Completeness [%] | 99.6 | 100 |
| Redundancy | 3.8 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.9 | SEE REFERENCE 3, pH 7.90 |
