4A91
Crystal structure of the glutamyl-queuosine tRNAAsp synthetase from E. coli complexed with L-glutamate
Replaces: 2ZLZExperimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 4 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 39.100, 115.030, 154.400 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.353 - 1.750 |
R-factor | 0.1662 |
Rwork | 0.165 |
R-free | 0.19880 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1nzj |
RMSD bond length | 0.006 |
RMSD bond angle | 0.981 |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 38.000 | 1.800 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.050 | 0.100 |
Number of reflections | 35738 | |
<I/σ(I)> | 25.4 | 7 |
Completeness [%] | 96.1 | 75.5 |
Redundancy | 3.72 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 0.1 M MG-ACETATE AND NA-CACODYLATE BUFFER (PH 5.5), 0.2 M KCL, 10% POLYETHYLENE GLYCOL 8000, AND 2 MM L-GLU. |