6E7X
Heterodimer of the GluN1b-GluN2B NMDA receptor amino-terminal domains bound to allosteric inhibitor 93-97
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-11-22 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0332 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 268.420, 59.536, 146.114 |
| Unit cell angles | 90.00, 116.69, 90.00 |
Refinement procedure
| Resolution | 25.000 - 2.580 |
| R-factor | 0.1867 |
| Rwork | 0.185 |
| R-free | 0.21630 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3qel |
| RMSD bond length | 0.001 |
| RMSD bond angle | 0.389 |
| Data reduction software | DENZO |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 35.000 | 35.000 | 2.620 |
| High resolution limit [Å] | 2.580 | 6.990 | 2.580 |
| Rmerge | 0.114 | 0.035 | 0.860 |
| Rmeas | 0.130 | 0.040 | 0.991 |
| Rpim | 0.061 | 0.018 | 0.480 |
| Total number of observations | 282558 | ||
| Number of reflections | 63551 | 3278 | 2932 |
| <I/σ(I)> | 8.1 | ||
| Completeness [%] | 96.2 | 94.2 | 89.9 |
| Redundancy | 4.4 | 4.5 | 4 |
| CC(1/2) | 0.998 | 0.548 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 290 | 3.0-3.5 M sodium formate, 0.1 M HEPES, 35 mM sodium chloride, 7 mM Tris-HCl, 50 uM Ifenprodil |
