4GDX
Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex
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 | 105.524, 125.247, 104.468 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.070 - 1.670 |
| R-factor | 0.1466 |
| Rwork | 0.145 |
| R-free | 0.17450 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2dbu |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.261 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: dev_1108)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.070 | 1.760 |
| High resolution limit [Å] | 1.670 | 1.670 |
| Rmerge | 0.076 | 0.740 |
| Number of reflections | 70751 | |
| <I/σ(I)> | 16.2 | 2.1 |
| Completeness [%] | 98.3 | 90.2 |
| Redundancy | 6.3 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 17.5% PEG3350, 100 mM Ammonium chloride, 0.5 mM L-glutamate, and 100 mM Na:Cacodylate pH 6.0 , VAPOR DIFFUSION, HANGING DROP, temperature 298K |
