1H23
Structure of acetylcholinesterase (E.C. 3.1.1.7) complexed with (S,S)-(-)-bis(12)-hupyridone at 2.15A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH3R |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-09-05 |
| Detector | RIGAKU IMAGE PLATE |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 111.794, 111.794, 137.775 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.300 - 2.150 |
| R-factor | 0.1893 |
| Rwork | 0.189 |
| R-free | 0.21500 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ace |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.940 * |
| 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] | 29.300 | 2.230 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.066 | 0.396 |
| Total number of observations | 536295 * | |
| Number of reflections | 54392 * | |
| <I/σ(I)> | 13.5 | |
| Completeness [%] | 99.7 | 99.8 |
| Redundancy | 0.38 | 9.79 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 5.8 | 4 * | PROTEIN WAS CRYSTALLISED FROM 28-30% V/V PEG 200 0.5M MES PH 5.8 AT 4 DEG. CELSIUS; THEN SOAKED IN IN MOTHER LIQUOR (40% V/V PEG 200 IN 0.1 M MES BUFFER, PH 5.8) CONTAINING 10MM (S,S)-(-)-BIS(12)-HUPYRIDONE DIHYDROCHLORIDE FOR 2 DAYS |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | PEG200 | 40 (%(v/v)) | |
| 2 | 1 | drop | MES | 0.5 (M) | pH5.8 |
| 3 | 1 | reservoir | PEG200 | 28-30 (%(v/v)) | |
| 4 | 1 | reservoir | MES | 0.5 (M) | pH5.8 |
