2ZJU
Crystal Structure of Lymnaea stagnalis Acetylcholine Binding Protein (Ls-AChBP) Complexed with Imidacloprid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 90 |
| Detector technology | CCD |
| Collection date | 2007-07-01 |
| Detector | Bruker DIP-6040 |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 65 |
| Unit cell lengths | 74.965, 74.965, 351.014 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 15.780 - 2.580 |
| R-factor | 0.203 |
| Rwork | 0.203 |
| R-free | 0.27700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1uw6 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.300 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | CNS (1.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.780 | 2.700 |
| High resolution limit [Å] | 2.560 | 2.560 |
| Rmerge | 0.080 | 0.413 |
| Number of reflections | 33040 | |
| <I/σ(I)> | 8.1 | 3.6 |
| Completeness [%] | 94.8 | 96.7 |
| Redundancy | 2.6 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.7 | 293 | 0.2M Na citrate, pH5.7, 15-22% PEG3350, 0.5mM imidacloprid, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
