1E7Z
Crystal structure of the EMAP2/RNA binding domain of the p43 protein from human aminoacyl-tRNA synthetase complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-04-26 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 36.141, 53.938, 41.371 |
| Unit cell angles | 90.00, 111.92, 90.00 |
Refinement procedure
| Resolution | 28.480 - 2.050 |
| R-factor | 0.221 |
| Rwork | 0.221 |
| R-free | 0.27200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fl0 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 25.500 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS (1.0) |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.042 * | 0.183 * |
| Total number of observations | 119628 * | |
| Number of reflections | 11716 | |
| <I/σ(I)> | 16.7 | |
| Completeness [%] | 99.4 | 96.5 |
| Redundancy | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 | pH 7.50 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 11 (mg/ml) | |
| 2 | 1 | reservoir | PEG3000 | 28-35 (%) | or PEG6000 |
| 3 | 1 | reservoir | Tris | 100 (mM) | |
| 4 | 1 | reservoir | 100-300 (mM) | ||
| 5 | 1 | reservoir | dithiothreitol | 2 (mM) |
