6E7T
Heterodimer of the GluN1b-GluN2B NMDA receptor amino-terminal domains bound to allosteric inhibitor 93-6
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS-II BEAMLINE 17-ID-2 |
| Synchrotron site | NSLS-II |
| Beamline | 17-ID-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-02-02 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9100 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 268.594, 59.835, 146.015 |
| Unit cell angles | 90.00, 116.86, 90.00 |
Refinement procedure
| Resolution | 25.000 - 2.310 |
| R-factor | 0.1953 |
| Rwork | 0.194 |
| R-free | 0.22500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3qel |
| RMSD bond length | 0.001 |
| RMSD bond angle | 0.363 |
| Data reduction software | DENZO |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.350 |
| High resolution limit [Å] | 2.310 | 6.270 | 2.310 |
| Rmerge | 0.092 | 0.037 | 0.606 |
| Rmeas | 0.107 | 0.042 | 0.770 |
| Rpim | 0.054 | 0.020 | 0.467 |
| Total number of observations | 299032 | ||
| Number of reflections | 83106 | 4763 | 2150 |
| <I/σ(I)> | 7.7 | ||
| Completeness [%] | 91.0 | 99.4 | 48.1 |
| Redundancy | 3.6 | 4.3 | 1.9 |
| CC(1/2) | 0.996 | 0.657 |
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 |
