6Q54
Structure of GluA2 ligand-binding domain (S1S2J) in complex with the agonist (S)-2-Amino-3-(1-ethyl-4-hydroxy-1H-1,2,3-triazol-5-yl)propanoic acid at 1.4 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX IV BEAMLINE BioMAX |
| Synchrotron site | MAX IV |
| Beamline | BioMAX |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-02-01 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.979988 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 98.331, 121.738, 47.134 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.954 - 1.400 |
| R-factor | 0.1451 |
| Rwork | 0.144 |
| R-free | 0.16330 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1m5b |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.149 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.3.22) |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 45.590 | 45.590 | 1.480 |
| High resolution limit [Å] | 1.400 | 4.430 | 1.400 |
| Rmerge | 0.032 | 0.458 | |
| Rmeas | 0.058 | 0.034 | 0.496 |
| Rpim | 0.022 | 0.013 | 0.189 |
| Number of reflections | 112106 | 3847 | 16195 |
| <I/σ(I)> | 16.1 | 15.6 | 1.6 |
| Completeness [%] | 100.0 | 99.7 | 99.9 |
| Redundancy | 6.8 | 6.5 | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 279 | 20% PEG4000, 0.3 M lithium sulfate, 0.1 M phosphate-citrate |
