3T93
Glutamate bound to a double cysteine mutant (A452C/S652C) of the ligand binding domain of GluA2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE A1 |
| Synchrotron site | CHESS |
| Beamline | A1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-03-09 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.977 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 47.551, 114.253, 163.804 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.951 - 1.907 |
| R-factor | 0.1828 |
| Rwork | 0.181 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3dp6 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.541 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.083 | 0.443 |
| Number of reflections | 69191 | |
| <I/σ(I)> | 22.13 | 3.239 |
| Completeness [%] | 98.3 | 98.6 |
| Redundancy | 5.2 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | 14-15% PEG8000, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
