1E66
STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH (-)-HUPRINE X AT 2.1A RESOLUTION
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X12C |
| Synchrotron site | NSLS |
| Beamline | X12C |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-08-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 112.335, 112.335, 138.165 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 40.000 * - 2.100 |
| R-factor | 0.176 * |
| Rwork | 0.177 |
| R-free | 0.20500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ace |
| RMSD bond length | 0.012 |
| RMSD bond angle | 23.300 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.420 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.060 * | 0.270 * |
| Total number of observations | 482340 * | |
| Number of reflections | 45140 * | |
| <I/σ(I)> | 16 | 2.24 |
| Completeness [%] | 76.0 | 20 * |
| Redundancy | 11.6 | 3.52 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.5 * | 4 * | PROTEIN WAS CRYSTALLISED FROM 35-40% W/V PEG 200 0.3M MES PH 5.6 4 DEG. CELSIUS |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | enzyme | 10-11 (mg/ml) | |
| 2 | 1 | drop | MES | 1 (mM) | pH6.5 |
| 3 | 1 | drop | 100 (mM) | ||
| 4 | 1 | drop | 0.02 (%) | ||
| 5 | 1 | reservoir | PEG200 | 40 (%) | |
| 6 | 1 | reservoir | MES | 0.3 (M) | pH5.8 |
