4A16
Structure of mouse Acetylcholinesterase complex with Huprine derivative
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2010-04-15 |
| Detector | ADSC QUANTUM 210 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 137.940, 171.930, 225.320 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.720 - 2.650 |
| R-factor | 0.15667 |
| Rwork | 0.155 |
| R-free | 0.20563 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1maa |
| RMSD bond length | 0.023 |
| RMSD bond angle | 2.138 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.700 |
| High resolution limit [Å] | 2.650 | 2.650 |
| Rmerge | 0.010 | 0.070 |
| Number of reflections | 155235 | |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 5.7 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 9 | 0.1 M BICINE BUFFER PH 9, 1.6 M AMMONIUM SULFATE. |
