5F06
Crystal structure of glutathione transferase F7 from Populus trichocarpa
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 |
Collection date | 2013-06-17 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.979769 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.104, 90.365, 97.149 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.420 - 1.800 |
R-factor | 0.1807 |
Rwork | 0.179 |
R-free | 0.21210 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4ri6 |
RMSD bond length | 0.006 |
RMSD bond angle | 0.861 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.570 | 1.820 |
High resolution limit [Å] | 1.730 | 1.730 |
Rmerge | 0.103 | 0.664 |
Number of reflections | 50544 | |
<I/σ(I)> | 13.1 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 7.3 | 7.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 7.5 | 277 | 16% PEG 4000, 10% 2-propanol, Na Hepes pH 7.5, 0.2 AS |