6F25
Crystal structure of human acetylcholinesterase in complex with C35.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-07-21 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.87313 |
| Spacegroup name | P 61 |
| Unit cell lengths | 211.074, 211.074, 115.725 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 48.889 - 3.052 |
| R-factor | 0.179826801437 |
| Rwork | 0.178 |
| R-free | 0.21416 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3lii |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.734 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.890 | 3.160 |
| High resolution limit [Å] | 3.050 | 3.050 |
| Rmerge | 0.053 | 0.661 |
| Rmeas | 0.075 | 0.934 |
| Number of reflections | 55240 | |
| <I/σ(I)> | 11.6 | |
| Completeness [%] | 98.9 | |
| Redundancy | 11.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 1.5 M LiSo4, 100 mM Hepes pH 7, 60 mM MgSo4 |
