3SH1
Ac-AChBP ligand binding domain mutated to human alpha-7 nAChR
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-02-03 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 85.793, 140.183, 136.806 |
| Unit cell angles | 90.00, 105.20, 90.00 |
Refinement procedure
| Resolution | 48.054 - 2.900 |
| R-factor | 0.214 |
| Rwork | 0.213 |
| R-free | 0.25800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Modified via pymol PDB entry 2BYR |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.442 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CCP4 (Program Suite 6.1.3) |
| Refinement software | PHENIX ((phenix.refine: 1.7_650)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.950 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.138 | 0.952 |
| Number of reflections | 85106 | |
| <I/σ(I)> | 13.909 | 1.5 |
| Completeness [%] | 73.4 | 95.7 |
| Redundancy | 7.5 | 6.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 290 | 30%MPD, 0.1M Na Cacodylate, 0.2M Magnesium Acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
