4HI7
Crystal structure of glutathione transferase homolog from drosophilia mojavensis, TARGET EFI-501819, with bound glutathione
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 31-ID |
Synchrotron site | APS |
Beamline | 31-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-08-13 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 0.9793 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 50.700, 50.700, 289.473 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.104 - 1.250 |
R-factor | 0.2013 |
Rwork | 0.200 |
R-free | 0.22780 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2il3 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.407 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.20) |
Phasing software | PHENIX (1.8_1069) |
Refinement software | PHENIX (1.8_1069) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 96.491 | 3.950 | 1.320 |
High resolution limit [Å] | 1.250 | 2.800 | 1.250 |
Rmerge | 0.073 | 0.053 | 0.457 |
Total number of observations | 51136 | 55616 | |
Number of reflections | 116694 | ||
<I/σ(I)> | 10.8 | 11.3 | 1.7 |
Completeness [%] | 96.1 | 99.5 | 91.6 |
Redundancy | 4.7 | 7.1 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | sitting drop vapor diffution | 6.5 | 298 | Protein (10 mM Hepes pH 7.5, 100 mM NaCl), Reservoir (0.2 M NaCl, 0.1 M Tris-CL pH 6.5, 30% PEG3000), Cryoprotection (reservoir + 20% ethylene glycol), sitting drop vapor diffution, temperature 298K |