2JF0
Mus musculus acetylcholinesterase in complex with tabun and Ortho-7
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I711 |
| Synchrotron site | MAX II |
| Beamline | I711 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-10-28 |
| Detector | MARRESERACH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 76.730, 108.580, 220.580 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.950 - 2.500 |
| R-factor | 0.206 |
| Rwork | 0.205 |
| R-free | 0.25100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1j06 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.452 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.150 | 2.640 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.090 | 0.510 |
| Number of reflections | 64151 | |
| <I/σ(I)> | 19.6 | 4.8 |
| Completeness [%] | 99.4 | 99.1 |
| Redundancy | 7.5 | 7.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 27-30 % PEG750MME, 0.1 M HEPES PH 7.0 |
