1GPN
STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH HUPERZINE B AT 2.35A RESOLUTION
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 120 |
| Detector technology | CCD |
| Collection date | 2000-05-10 |
| Detector | BRUKER-AXS |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 111.722, 111.722, 137.124 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.350 |
| R-factor | 0.1862 |
| Rwork | 0.186 |
| R-free | 0.21600 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ea5 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.529 |
| 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] | 20.000 | 2.430 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmerge | 0.058 | 0.225 |
| Total number of observations | 159761 * | |
| Number of reflections | 41627 | |
| <I/σ(I)> | 14.9 | 3.6 |
| Completeness [%] | 98.3 | 99.7 |
| Redundancy | 15.9 | 16 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 5.8 * | 4 * | Raves, M.L., (1997) Nature Struct. Biol., 4, 57. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG200 | 38 (%) | |
| 2 | 1 | reservoir | MES | 0.1 (M) | |
| 3 | 1 | drop | protein | 12 (mg/ml) |
