4GG2
The crystal structure of glutamate-bound human gamma-glutamyltranspeptidase 1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2011-10-18 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.1 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 105.717, 126.753, 104.629 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.975 - 2.210 |
| R-factor | 0.142 |
| Rwork | 0.140 |
| R-free | 0.18330 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4gdx |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.343 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((phenix.refine: dev_1120)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.180 | 2.240 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.108 | 0.563 |
| Number of reflections | 34317 | |
| <I/σ(I)> | 31.3 | 3.6 |
| Completeness [%] | 97.2 | 75.8 |
| Redundancy | 18.5 | 10.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | 15-25% PEG3350, 100 mM Ammonium chloride, 0.5 mM L-glutamate, 100 mM Na:Cacodylate pH 6.0 , VAPOR DIFFUSION, HANGING DROP, temperature 298K |
