5CHE
Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its regulatory proteins
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-01-19 |
Detector | RAYONIX MX-325 |
Wavelength(s) | 0.9793 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 216.994, 53.211, 203.763 |
Unit cell angles | 90.00, 108.36, 90.00 |
Refinement procedure
Resolution | 39.265 - 3.203 |
R-factor | 0.2255 |
Rwork | 0.223 |
R-free | 0.27790 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4n7r 4yvq |
RMSD bond length | 0.006 |
RMSD bond angle | 0.975 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8.1_1168)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.310 |
High resolution limit [Å] | 3.200 | 3.200 |
Rmerge | 0.132 | 0.831 |
Number of reflections | 36775 | |
<I/σ(I)> | 10 | 1.68 |
Completeness [%] | 99.6 | 99.9 |
Redundancy | 4.3 | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 7 | 289 | PEG 3350, sodium malonate, LiCl, MPD |