5F05
Crystal structure of glutathione transferase F5 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 | 2014-04-12 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.979961 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 54.459, 85.952, 88.520 |
Unit cell angles | 90.00, 97.93, 90.00 |
Refinement procedure
Resolution | 43.350 - 1.700 |
R-factor | 0.1459 |
Rwork | 0.144 |
R-free | 0.18090 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4ri6 |
RMSD bond length | 0.015 |
RMSD bond angle | 1.542 |
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] | 49.060 | 1.790 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.102 | 0.565 |
Number of reflections | 88400 | |
<I/σ(I)> | 11 | 3 |
Completeness [%] | 99.6 | 92 |
Redundancy | 3.8 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 8.5 | 277 | 30% PEG 4000, Tris HCl, 0.2 M Mg chloride |