1VXR
O-ETHYLMETHYLPHOSPHONYLATED ACETYLCHOLINESTERASE OBTAINED BY REACTION WITH O-ETHYL-S-[2-[BIS(1-METHYLETHYL)AMINO]ETHYL] METHYLPHOSPHONOTHIOATE (VX)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-08-22 |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 112.836, 112.836, 137.360 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 2.200 |
| R-factor | 0.189 * |
| Rwork | 0.189 |
| R-free | 0.23000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ace |
| RMSD bond length | 0.023 |
| RMSD bond angle | 24.000 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Number of reflections | 47840 | |
| <I/σ(I)> | 12.7 | 1.6 |
| Completeness [%] | 92.3 | 83.9 |
| Redundancy | 8.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6 | 4 * | Millard, C.B., (1999) Biochemistry, 38, 7032. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | PEG200 | 35-40 (%(w/v)) | |
| 3 | 1 | reservoir | MES | 0.15 (M) | |
| 4 | 1 | reservoir | 0.05 (M) |
