4KCC
Crystal Structure of the NMDA Receptor GluN1 Ligand Binding Domain Apo State
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 | 2012-04-12 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.00000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 87.269, 66.359, 63.468 |
| Unit cell angles | 90.00, 105.21, 90.00 |
Refinement procedure
| Resolution | 36.849 - 1.894 |
| R-factor | 0.1735 |
| Rwork | 0.172 |
| R-free | 0.20560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1pb7 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.287 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.078 | 0.560 |
| Number of reflections | 27791 | |
| <I/σ(I)> | 17.6 | 2.5 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 3.8 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | 0.2 M NaKphosphate, 20% PEG 3350, 2% glycerol, 0.2 M NaCl, 0.01 M Tris, 0.001 M EDTA, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
