5A3V
Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 315r |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 44.720, 142.650, 209.890 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.267 - 2.340 |
R-factor | 0.1849 |
Rwork | 0.181 |
R-free | 0.25050 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.350 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 42.267 | 2.490 |
High resolution limit [Å] | 2.340 | 2.340 |
Rmerge | 0.134 | 0.471 |
Number of reflections | 28266 | |
<I/σ(I)> | 13.24 | 2.69 |
Completeness [%] | 97.6 | 87.6 |
Redundancy | 6.64 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 0.2 M SODIUM ACETATE, 0.1 M TRIS-HCL PH 8.5, 32% PEG4000 (V/V) |