4X5T
alpha 1 glycine receptor transmembrane structure fused to the extracellular domain of GLIC
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-09-08 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97250 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 118.894, 132.304, 190.517 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.000 - 3.500 |
| R-factor | 0.2543 |
| Rwork | 0.254 |
| R-free | 0.27000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hfi |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.160 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.11.4) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.420 | 3.690 |
| High resolution limit [Å] | 3.500 | 3.500 |
| Rmerge | 0.081 | 1.410 |
| Number of reflections | 38553 | |
| <I/σ(I)> | 12.8 | 0.638 |
| Completeness [%] | 99.8 | 99.9 |
| Redundancy | 4.9 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 3 | 291 | 16 % PEG 2000MME, 50 mM NiCl2, 4% DMSO, 11% ethylene glycol and 0.1 M NaAcetate pH 3.0 |
