1OCE
ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH MF268
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE AREA DETECTOR |
| Collection date | 1997-06 |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 111.496, 111.496, 137.390 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 8.000 - 2.700 |
| R-factor | 0.208 |
| Rwork | 0.208 |
| R-free | 0.29100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ace |
| RMSD bond length | 0.008 |
| RMSD bond angle | 27.100 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.140 * | 0.648 * |
| Total number of observations | 248837 * | |
| Number of reflections | 24049 | 1886 * |
| <I/σ(I)> | 6.7 | 1.7 |
| Completeness [%] | 87.2 | 69.7 |
| Redundancy | 2.3 | 1.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6 | Sussman, J.L., (1988) J. Mol. Biol., 203, 821. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG200 | 35 (%) | |
| 2 | 1 | drop | protein | 8-10 (mg/ml) | |
| 3 | 1 | drop | PEG200 | 18 (%) | |
| 4 | 1 | drop | MES | 0.5 (M) |
