5ICT
Crystal structure of the Drosophila GluR1A ligand binding domain Y792T mutant complex with glutamate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-02-15 |
| Detector | RAYONIX MX300-HS |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 53.208, 58.406, 99.802 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.203 - 1.680 |
| R-factor | 0.1476 |
| Rwork | 0.146 |
| R-free | 0.17230 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5dt6 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.018 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.710 |
| High resolution limit [Å] | 1.680 | 1.680 |
| Rmerge | 0.031 | 0.340 |
| Number of reflections | 36199 | |
| <I/σ(I)> | 34.2 | 2.8 |
| Completeness [%] | 98.9 | 88.1 |
| Redundancy | 6.3 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | Sample buffer 150 NaCl, 10 Tris pH 8.5, 5 Na Glutamate, 1 mM EDTA, 10% glycerol Reservoir 12% PEG 8K, 100 Tris pH 8.5 |
