2BR7
Crystal Structure of Acetylcholine-binding Protein (AChBP) from Aplysia californica in complex with HEPES
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 | I 2 3 |
| Unit cell lengths | 204.203, 204.203, 204.203 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.840 - 3.000 |
| R-factor | 0.178 |
| Rwork | 0.174 |
| R-free | 0.24900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ux2 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.506 |
| 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 | 3.160 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.160 | 0.490 |
| Number of reflections | 28431 | |
| <I/σ(I)> | 4.5 | 1.5 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 8.1 | 8.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 100 MM HEPES 1.15 M SODIUM MALONATE, pH 7.00 |
