2PVQ
Crystal structure of Ochrobactrum anthropi glutathione transferase Cys10Ala mutant with glutathione bound at the H-site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-06-19 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.934 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 58.373, 58.373, 214.023 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 50.640 - 1.803 |
| R-factor | 0.20006 |
| Rwork | 0.198 |
| R-free | 0.24772 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 2nto |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.303 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | FFT |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.640 | 1.860 |
| High resolution limit [Å] | 1.803 | 1.803 |
| Rmerge | 0.085 | 0.401 |
| Number of reflections | 20967 | |
| <I/σ(I)> | 16 | 3.51 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 66.6 | 8.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 294 | 2.0 M ammonium sulfate, 100 mM Tris-HCl, 200 mM Lithium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
