2NTO
Structure of the Glutathione Transferase from Ochrobactrum anthropi in complex with glutathione
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-07-02 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.934 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 58.765, 58.765, 212.323 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 50.640 - 2.095 |
| R-factor | 0.18955 |
| Rwork | 0.187 |
| R-free | 0.23181 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1a0f |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.307 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.640 | 2.180 |
| High resolution limit [Å] | 2.095 | 2.095 |
| Rmerge | 0.070 | 0.335 |
| Number of reflections | 13632 | |
| <I/σ(I)> | 11.8 | 8.41 |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 13.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 294 | 2.0 M Ammonium Sulphate, 0.1 M Tris pH 7.0, 0.2 M lithium sulphate, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
