1GPK
Structure of Acetylcholinesterase Complex with (+)-Huperzine A at 2.1A Resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-05-10 |
Detector | BRUKER-AXS |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 111.421, 111.421, 137.145 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.100 |
R-factor | 0.1886 |
Rwork | 0.189 |
R-free | 0.21400 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ea5 |
RMSD bond length | 0.006 |
RMSD bond angle | 1.320 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.044 | 0.416 * |
Total number of observations | 677200 * | |
Number of reflections | 57502 * | |
<I/σ(I)> | 15.2 | 2 |
Completeness [%] | 98.8 | 99.9 |
Redundancy | 2.3 |
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) |