2HA4
Crystal structure of mutant S203A of mouse acetylcholinesterase complexed with acetylcholine
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 | 2004-06-25 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.933 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 79.671, 111.730, 228.159 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.560 |
| R-factor | 0.1898 |
| Rwork | 0.189 |
| R-free | 0.22401 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 1j06 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.301 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.650 |
| High resolution limit [Å] | 2.560 | 2.560 |
| Rmerge | 0.062 | 0.383 |
| Number of reflections | 65686 | |
| <I/σ(I)> | 13 | 3.4 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 3.7 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
