3WTO
Crystal Structure of Lymnaea stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Desnitro-imidacloprid
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B2 |
Synchrotron site | SPring-8 |
Beamline | BL26B2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-07-03 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.9 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 73.056, 120.742, 139.346 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.780 - 2.250 |
R-factor | 0.215 |
Rwork | 0.215 |
R-free | 0.26200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2zju |
RMSD bond length | 0.007 |
RMSD bond angle | 1.400 |
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 | 2.330 |
High resolution limit [Å] | 2.250 | 2.250 |
Rmerge | 0.076 | 0.449 |
Number of reflections | 58935 | |
<I/σ(I)> | 38.2 | 4.9 |
Completeness [%] | 99.8 | 99.7 |
Redundancy | 7.3 | 7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 8.5 | 293 | 24-27 % PEG4000, 0.1-0.3M LiSO4, 0.1M Tris-HCl, pH 8.5, 0.5mM Desnitro-imidacloprid, VAPOR DIFFUSION, temperature 293K |