4YMA
Structure of the ligand-binding domain of GluA2 in complex with the antagonist CNG10109
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-3 |
| Synchrotron site | MAX II |
| Beamline | I911-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-12-13 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 48.880, 65.250, 91.550 |
| Unit cell angles | 90.00, 92.36, 90.00 |
Refinement procedure
| Resolution | 36.389 - 1.895 |
| R-factor | 0.1733 |
| Rwork | 0.170 |
| R-free | 0.22780 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3tza |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.000 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.3.20) |
| Phasing software | PHASER (2.5.1) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 91.472 | 36.389 | 2.000 |
| High resolution limit [Å] | 1.895 | 5.990 | 1.890 |
| Rmerge | 0.041 | 0.372 | |
| Rmeas | 0.095 | ||
| Rpim | 0.047 | 0.024 | 0.211 |
| Total number of observations | 190896 | 6100 | 27125 |
| Number of reflections | 45862 | ||
| <I/σ(I)> | 11.3 | 21.4 | 3.6 |
| Completeness [%] | 100.0 | 99.5 | 100 |
| Redundancy | 4.2 | 4 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 280 | PEG4000, lithium sulfate, phosphate citrate |
