6E7V
Heterodimer of the GluN1b-GluN2B NMDA receptor amino-terminal domains bound to allosteric inhibitor 93-88
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 | 268.131, 59.612, 145.526 |
| Unit cell angles | 90.00, 116.86, 90.00 |
Refinement procedure
| Resolution | 25.000 - 2.600 |
| R-factor | 0.1929 |
| Rwork | 0.191 |
| R-free | 0.23250 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3qel |
| RMSD bond length | 0.001 |
| RMSD bond angle | 0.346 |
| 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 | 2.640 |
| High resolution limit [Å] | 2.600 | 7.040 | 2.600 |
| Rmerge | 0.091 | 0.031 | 0.659 |
| Rmeas | 0.120 | 0.041 | 0.880 |
| Rpim | 0.078 | 0.027 | 0.579 |
| Total number of observations | 113979 | ||
| Number of reflections | 56531 | 3011 | 1999 |
| <I/σ(I)> | 5.8 | ||
| Completeness [%] | 88.6 | 89.5 | 63.8 |
| Redundancy | 2 | 2.1 | 1.6 |
| CC(1/2) | 0.996 | 0.624 |
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 |
