1CFJ
METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED) OBTAINED BY REACTION WITH O-ISOPROPYLMETHYLPHOSPHONOFLUORIDATE (GB, SARIN)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X12C |
| Synchrotron site | NSLS |
| Beamline | X12C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1997-07-01 |
| Detector | BRANDEIS - B4 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 111.395, 111.395, 136.623 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 2.600 |
| Rwork | 0.186 |
| R-free | 0.24700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ace |
| RMSD bond length | 0.020 * |
| RMSD bond angle | 24.200 * |
| 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 | 2.690 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.090 * | 0.170 * |
| Total number of observations | 200755 * | |
| Number of reflections | 30011 | |
| <I/σ(I)> | 10.3 | 2.2 |
| Completeness [%] | 97.4 | 99.3 |
| Redundancy | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6 | 4 * | 35-40% (W/V) PEG-200 0.15 M MES BUFFER PH 6, 0.05 M NACL, 4 DEG C , temperature 277.0K |
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 (%(v/v)) | |
| 3 | 1 | reservoir | MES | 0.15 (M) | |
| 4 | 1 | reservoir | 0.05 (M) |
