2C5F
Torpedo californica acetylcholinesterase in complex with a non hydrolysable substrate analogue, 4-oxo-N,N,N-trimethylpentanaminium
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-03-05 |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 112.260, 112.260, 137.000 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.600 |
| R-factor | 0.1626 |
| Rwork | 0.163 |
| R-free | 0.21950 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ea5 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.335 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | CNS |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.700 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.080 | 0.300 |
| Number of reflections | 30595 | |
| <I/σ(I)> | 16.12 | 5.92 |
| Completeness [%] | 97.8 | 97 |
| Redundancy | 5.98 | 5.59 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | 277 | 32% PEG200, 150MM MES, PH6, 4 DEG. C, pH 6.00 |
