5G5F
Crystallographic structure of the Tau class glutathione S-transferase MiGSTU in complex with reduced glutathione.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SEALED TUBE |
Source details | BRUKER D8 QUEST |
Temperature [K] | 100 |
Detector technology | CMOS |
Collection date | 2015-12-04 |
Detector | BRUKER |
Wavelength(s) | 1.54178 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 87.483, 48.240, 52.684 |
Unit cell angles | 90.00, 104.16, 90.00 |
Refinement procedure
Resolution | 20.277 - 2.300 |
R-factor | 0.1976 |
Rwork | 0.193 |
R-free | 0.24290 |
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 | 0.006 |
RMSD bond angle | 1.035 |
Data reduction software | PROTEUM2 |
Data scaling software | SADABS |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.300 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.040 | 0.300 |
Number of reflections | 9224 | |
<I/σ(I)> | 25 | 4.3 |
Completeness [%] | 96.3 | 97.6 |
Redundancy | 2 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6 | 0.2 M AMMONIUM ACETATE, 0.1 M BIS-TRIS PH 6.0, 25%(W/V) POLYETHYLENE GLYCOL 3350, 5 MM GSH |