5NF5
Structure of GluK1 ligand-binding domain (S1S2) in complex with CIP-AS at 2.85 A resolution
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 | 2015-06-18 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 70.334, 70.334, 231.913 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.710 - 2.850 |
| R-factor | 0.213 |
| Rwork | 0.210 |
| R-free | 0.26100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4e0x |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.615 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.3.20) |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.630 | 3.000 |
| High resolution limit [Å] | 2.850 | 2.850 |
| Rmerge | 0.480 | |
| Number of reflections | 14455 | |
| <I/σ(I)> | 19.4 | 1.6 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 10.7 | 11.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 279 | 24.4% PEG4000, 0.3 M lithium sulfate, 0.1 M cacodylate buffer pH 6.5 |
