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) |