5F0G
Structure of the glutathione transferase delta 2 from Drosophila melanogaster
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-07-05 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.978 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 47.500, 87.500, 53.200 |
Unit cell angles | 90.00, 113.90, 90.00 |
Refinement procedure
Resolution | 19.950 - 1.600 |
R-factor | 0.1739 |
Rwork | 0.172 |
R-free | 0.21710 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ein |
RMSD bond length | 0.011 |
RMSD bond angle | 1.274 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.950 | 1.640 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.060 | |
Number of reflections | 51278 | |
<I/σ(I)> | 15.09 | 2.03 |
Completeness [%] | 97.6 | 97 |
Redundancy | 3.38 | 3.38 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4 | 293 | 0.1 M succinic acid, phosphate, glycin (SPG buffer), 25% PEG 1500, pH = 4 |