5CFB
Crystal Structure of Human Glycine Receptor alpha-3 Bound to Strychnine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-02-25 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 140.242, 143.198, 180.054 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 3.040 |
| R-factor | 0.2615 |
| Rwork | 0.260 |
| R-free | 0.28260 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4tnv |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.060 |
| Data scaling software | SCALEPACK (0.98) |
| Phasing software | PHASER (2.5.6) |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 3.110 |
| High resolution limit [Å] | 3.000 | 6.460 | 3.000 |
| Rmerge | 0.201 | 0.165 | |
| Rmeas | 0.211 | 0.173 | |
| Rpim | 0.064 | 0.050 | 0.453 |
| Total number of observations | 684083 | ||
| Number of reflections | 68041 | ||
| <I/σ(I)> | 5.3 | ||
| Completeness [%] | 97.8 | 99.7 | 85.4 |
| Redundancy | 10.1 | 10.7 | 5.8 |
| CC(1/2) | 0.983 | 0.560 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4 | 277 | 30-33% PEG-400, 200 mM magnesium chloride, 100 mM potassium chloride, 25 mM sodium citrate |
