4KDX
Crystal structure of a glutathione transferase family member from burkholderia graminis, target efi-507264, bound gsh, ordered domains, space group p21, form(1)
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 | 2013-04-17 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 65.844, 56.107, 67.317 |
| Unit cell angles | 90.00, 108.38, 90.00 |
Refinement procedure
| Resolution | 24.320 - 1.350 |
| R-factor | 0.148 |
| Rwork | 0.148 |
| R-free | 0.16700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4iel |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.316 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 200.000 | 1.370 |
| High resolution limit [Å] | 1.350 | 1.350 |
| Rmerge | 0.061 | 0.590 |
| Number of reflections | 93495 | |
| <I/σ(I)> | 19.9 | 2 |
| Completeness [%] | 91.5 | 48 |
| Redundancy | 3.5 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 298 | Protein (10 mM Hepes, 150 mM NaCl, 5% glycerol, 5 mM GSH); Reservoir (0.2 M AmmoniumAcetate 0.1 M HEPES pH 7.5 25 %(w/v) PEG 3350); Cryoprotection (reservoir + 20% glycerol) , VAPOR DIFFUSION, SITTING DROP, temperature 298K |
