5H8F
Structure of the apo human GluN1/GluN2A LBD
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-11-19 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.268, 89.193, 124.739 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.440 - 1.810 |
| R-factor | 0.178 |
| Rwork | 0.176 |
| R-free | 0.20690 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2a5t |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.010 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.11.5) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.870 |
| High resolution limit [Å] | 1.810 | 1.810 |
| Rmerge | 0.030 | 0.577 |
| Number of reflections | 55343 | |
| <I/σ(I)> | 21.9 | 2.9 |
| Completeness [%] | 99.2 | 98.4 |
| Redundancy | 4.9 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | 1:2 v/v protein to mother liquor (0.1 M HEPES, pH 7.0, 10-13% PEG8000, 2 mM calcium acetate) |
