8OWM
Crystal structure of glutamate dehydrogenase 2 from Arabidopsis thaliana binding Ca, NAD and 2,2-dihydroxyglutarate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1) |
Synchrotron site | PETRA III, EMBL c/o DESY |
Beamline | P13 (MX1) |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-06-21 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.976200 |
Spacegroup name | P 1 |
Unit cell lengths | 95.544, 95.629, 95.841 |
Unit cell angles | 90.42, 93.59, 117.78 |
Refinement procedure
Resolution | 65.700 - 1.700 |
R-factor | 0.1441 |
Rwork | 0.144 |
R-free | 0.17210 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6yei |
RMSD bond length | 0.009 |
RMSD bond angle | 0.995 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.18.1_3865) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 65.700 | 1.800 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.062 | 0.758 |
Rmeas | 0.075 | 0.927 |
Number of reflections | 318817 | 50659 |
<I/σ(I)> | 10.76 | 1.32 |
Completeness [%] | 96.9 | 95.2 |
Redundancy | 3.55 | 2.92 |
CC(1/2) | 0.998 | 0.624 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 273 | 0.12MMonosaccharides (0.02M D-Glucose; 0.02M D-Mannose; 0.02M D-Galactose; 0.02M L-Fucose; 0.02M D-Xylose; 0.02M N-Acetyl-D-Glucosamine ),0.1M Imidazole/MES buffer pH 6.5, 20% v/v Glycerol and 10% w/v PEG 4000 |