5VIH
Crystal structure of GluN1/GluN2A NMDA receptor agonist binding domains with glycine and antagonist, 4-fluorophenyl-ACEPC
Replaces: 5DE4Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-06-12 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.987 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.736, 87.221, 122.277 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.985 - 2.400 |
R-factor | 0.2052 |
Rwork | 0.200 |
R-free | 0.27180 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4nf8 |
RMSD bond length | 0.003 |
RMSD bond angle | 0.609 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.980 | 2.180 |
High resolution limit [Å] | 2.400 | 2.110 |
Number of reflections | 25693 | |
<I/σ(I)> | 8.78 | 1.95 |
Completeness [%] | 98.1 | 86.4 |
Redundancy | 3 | 1.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | Ammonia Acetate, PEG 4000 |