5KEJ
Crystallographic structure of the Tau class glutathione S-transferase MiGSTU in complex with S-hexyl-glutathione
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL14-1 |
Synchrotron site | SSRL |
Beamline | BL14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-05-21 |
Detector | MARMOSAIC 325 mm CCD |
Wavelength(s) | 1.181 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 64.319, 88.805, 96.583 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.343 - 2.350 |
R-factor | 0.1895 |
Rwork | 0.188 |
R-free | 0.22610 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Homology model based on the structure of wheat Tau class glutathione S-transferase (PDB entry 1GWC). |
RMSD bond length | 0.010 |
RMSD bond angle | 1.219 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.343 | 2.480 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmerge | 0.170 | |
Number of reflections | 23652 | |
<I/σ(I)> | 11.8 | 3.3 |
Completeness [%] | 100.0 | 100 |
Redundancy | 14.6 | 14.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | BATCH MODE | 6 | 289 | 0.2 M ammonium acetate, 0.1 M Bis-Tris pH 6.0, 25%(w/v) polyethylene glycol 3350, 5 mM S-hexyl-glutathione |