2XI4
Torpedo californica Acetylcholinesterase in Complex with Aflatoxin B1 (Orthorhombic Space Group)
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 | 2007-09-10 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 91.730, 107.030, 150.730 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.220 - 2.300 |
| R-factor | 0.18244 |
| Rwork | 0.180 |
| R-free | 0.23366 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1w75 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.491 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.220 | 2.350 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.060 | 0.420 |
| Number of reflections | 65334 | |
| <I/σ(I)> | 23.07 | 4.57 |
| Completeness [%] | 98.1 | 100 |
| Redundancy | 6.05 | 5.94 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.8 | 277 | ACHE WAS CRYSTALLIZED IN 34% PEG200, 150 MM MES, PH 6, 4 DEG. C. THE CRYSTAL WAS SOAKED FOR 15 H IN 100 MICROMOLAR AFLATOXIN B1, 10% ETOH, 36% PEG200, 150MM MES, PH 5.8, 4 DEG C. |
