5SYO
Crystal structure of a chimeric acetylcholine binding protein from Aplysia californica (Ac-AChBP) containing loop C from the human alpha 3 nicotinic acetylcholine receptor in complex with Cytisine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.1 |
| Synchrotron site | ALS |
| Beamline | 5.0.1 |
| Temperature [K] | 90 |
| Detector technology | CCD |
| Collection date | 2012-05-13 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 68.596, 78.077, 120.343 |
| Unit cell angles | 90.00, 93.34, 90.00 |
Refinement procedure
| Resolution | 48.089 - 2.000 |
| R-factor | 0.2049 |
| Rwork | 0.204 |
| R-free | 0.22740 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4zk4 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.030 |
| High resolution limit [Å] | 2.000 | 5.430 | 2.000 |
| Rmerge | 0.063 | 0.035 | 0.267 |
| Total number of observations | 633024 | ||
| Number of reflections | 85774 | ||
| <I/σ(I)> | 13.1 | ||
| Completeness [%] | 99.9 | 99.9 | 99.3 |
| Redundancy | 7.4 | 7.5 | 7.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | 1.7% PEG 400, 0.085 M HEPES - Na pH 7.5, 1.7 M Ammonium Sulfate, 15% Glycerol |
