1MQD
X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-Des-Me-AMPA at 1.46 A resolution. Crystallization in the presence of lithium sulfate.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-08-15 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.84990 |
| Spacegroup name | P 1 2 1 |
| Unit cell lengths | 105.445, 47.505, 123.920 |
| Unit cell angles | 90.00, 113.70, 90.00 |
Refinement procedure
| Resolution | 20.000 * - 1.460 |
| Rwork | 0.180 |
| R-free | 0.19200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1m5b |
| RMSD bond length | 0.005 |
| RMSD bond angle | 22.400 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.490 |
| High resolution limit [Å] | 1.460 | 1.460 |
| Rmerge | 0.042 | 0.384 |
| Number of reflections | 191888 | |
| <I/σ(I)> | 26.7 | 2.4 |
| Completeness [%] | 99.0 | 95.5 |
| Redundancy | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.4 * | 6 * | 20% PEG 8000, 0.1M lithium sulfate, 0.1M cacodylate, pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 279K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 8 (mg/ml) | |
| 2 | 1 | drop | (S)-Des-Me-AMPA | 3 (mM) | |
| 3 | 1 | drop | HEPES | 10 (mM) | pH7.4 |
| 4 | 1 | drop | 20 (mM) | ||
| 5 | 1 | drop | EDTA | 1 (mM) | |
| 6 | 1 | reservoir | 0.1 (M) | ||
| 7 | 1 | reservoir | PEG8000 | 20 (%) | |
| 8 | 1 | reservoir | cacodylate | 0.1 (M) | pH5.2 |
