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 |
