2BR8
Crystal Structure of Acetylcholine-binding Protein (AChBP) from Aplysia californica in complex with an alpha-conotoxin PnIA variant
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 | 2004-09-30 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 67.473, 80.085, 134.043 |
| Unit cell angles | 90.00, 93.20, 90.00 |
Refinement procedure
| Resolution | 19.800 - 2.400 |
| R-factor | 0.201 |
| Rwork | 0.198 |
| R-free | 0.25000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ux2 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.532 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.520 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.100 | 0.400 |
| Number of reflections | 55263 | |
| <I/σ(I)> | 6 | 1.8 |
| Completeness [%] | 97.9 | 90.4 |
| Redundancy | 3.45 | 2.98 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 18 % PEG 3350, 180 MM NA2SO4, 100 MM BIS-TRIS PROPANE PH 7.5 |
