2C9T
Crystal Structure Of Acetylcholine Binding Protein (AChBP) From Aplysia Californica In Complex With alpha-Conotoxin ImI
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-06-18 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 113.211, 123.131, 118.749 |
| Unit cell angles | 90.00, 117.47, 90.00 |
Refinement procedure
| Resolution | 105.410 - 2.250 |
| R-factor | 0.171 |
| Rwork | 0.168 |
| R-free | 0.22700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2br8 |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.595 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 54.070 | 2.370 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.080 | 0.520 |
| Number of reflections | 135691 | |
| <I/σ(I)> | 14.2 | 2.8 |
| Completeness [%] | 99.2 | 98.8 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 100 MM SODIUM ACETATE PH 5.5, 12.5% PEG5000 MME |
