6E7S
Heterodimer of the GluN1b-GluN2B NMDA receptor amino-terminal domains bound to allosteric inhibitor 93-5
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 | 2017-03-08 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.91979 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 268.430, 60.633, 145.391 |
Unit cell angles | 90.00, 116.42, 90.00 |
Refinement procedure
Resolution | 25.000 - 2.720 |
R-factor | 0.1909 |
Rwork | 0.189 |
R-free | 0.23430 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3qel |
RMSD bond length | 0.001 |
RMSD bond angle | 0.379 |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.31) |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 29.880 | 29.880 | 2.790 |
High resolution limit [Å] | 2.720 | 12.160 | 2.720 |
Rmerge | 0.065 | 0.020 | 0.958 |
Rmeas | 0.077 | 0.024 | 1.152 |
Rpim | 0.041 | 0.012 | 0.632 |
Total number of observations | 2181 | 12596 | |
Number of reflections | 56030 | 633 | 3959 |
<I/σ(I)> | 14.4 | 50.7 | 1.4 |
Completeness [%] | 98.6 | 92 | 93.9 |
Redundancy | 3.5 | 3.4 | 3.2 |
CC(1/2) | 0.999 | 0.999 | 0.598 |
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 |