3WTN
Crystal Structure of Lymnaea stagnalis Acetylcholine Binding Protein Complexed with Desnitro-imidacloprid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL44B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-06-13 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 77.006, 118.401, 243.591 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.840 - 2.090 |
| R-factor | 0.213 |
| Rwork | 0.213 |
| R-free | 0.26200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2zju |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | CNS (1.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.180 |
| High resolution limit [Å] | 2.090 | 2.090 |
| Rmerge | 0.074 | 0.463 |
| Number of reflections | 131277 | |
| <I/σ(I)> | 2.8 | |
| Completeness [%] | 99.2 | 93.7 |
| Redundancy | 7.1 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | 293 | 1.5M Na acetate, 0.05M CdSO4, 0.1M HEPES-Na (pH 7.5), 0.5mM Desnitro-imidacloprid, VAPOR DIFFUSION, temperature 293K |
