5I56
Agonist-bound GluN1/GluN2A agonist binding domains with TCN201
Experimental 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 | 2015-12-06 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.98 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.259, 88.402, 126.146 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.030 - 2.280 |
R-factor | 0.188 |
Rwork | 0.184 |
R-free | 0.23900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4nf8 |
RMSD bond length | 0.004 |
RMSD bond angle | 0.844 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.032 | 2.360 |
High resolution limit [Å] | 2.278 | 2.280 |
Rmerge | 0.490 | |
Number of reflections | 27522 | |
<I/σ(I)> | 10.42 | |
Completeness [%] | 96.7 | 91.8 |
Redundancy | 4.7 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 0.2 M ammonium sulfate and 16-22% PEG 4000 |