1PGT
CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1[V104] COMPLEXED WITH S-HEXYLGLUTATHIONE
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | ENRAF-NONIUS FR571 |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-03 |
| Detector | MACSCIENCE |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 79.390, 90.800, 69.150 |
| Unit cell angles | 90.00, 98.08, 90.00 |
Refinement procedure
| Resolution | 6.000 - 1.800 |
| R-factor | 0.182 * |
| Rwork | 0.182 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gss |
| RMSD bond length | 0.015 |
| RMSD bond angle | 0.033 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | GPRLSA |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.057 | 0.303 |
| Number of reflections | 43132 | |
| <I/σ(I)> | 13.92 | 1.81 |
| Completeness [%] | 96.0 | 86.9 |
| Redundancy | 4.2 | 1.41 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | CRYSTALS WERE GROWN IN HANGING DROPS WHICH INITIALLY CONSISTED OF 5.9 MG/ML PROTEIN IN 0.1 M HEPES BUFFER (PH 6.5) CONTAINING 8.3 MM S-HEXYLGLUTATHIONE AND 1.0 M BUFFERED (PH 6.5) AMMONIUM SULFATE. THE DROPS WERE EQUILIBRATED AT 293 K AGAINST WELL SOLUTION CONTAINING BETWEEN 1.9 - 2.0 M AMMONIUM SULFATE IN 0.1 M HEPES BUFFER (PH 6.5)., vapor diffusion - hanging drop |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5.9 (mg/ml) | |
| 2 | 1 | drop | HEPES | 0.1 (M) | |
| 3 | 1 | drop | GSHex | 8.3 (mM) | |
| 4 | 1 | drop | ammonium sulfate | 1.0 (M) | |
| 5 | 1 | reservoir | ammonium sulfate | 1.9-2.0 (M) | |
| 6 | 1 | reservoir | HEPES | 0.1 (M) |
