3U8N
Crystal structure of the acetylcholine binding protein (AChBP) from Lymnaea stagnalis in complex with NS3950 (1-(6-bromo-5-ethoxypyridin-3-yl)-1,4-diazepane)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-2 |
| Synchrotron site | MAX II |
| Beamline | I911-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-03-19 |
| Detector | MAR CCD 165 mm |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 239.120, 73.110, 271.840 |
| Unit cell angles | 90.00, 97.45, 90.00 |
Refinement procedure
| Resolution | 33.050 - 2.350 |
| R-factor | 0.198 |
| Rwork | 0.197 |
| R-free | 0.23000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1UW6: PENTAMER CHAIN A-E |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.045 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.6.4_486)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.190 | 2.480 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmerge | 0.070 | 0.191 |
| Number of reflections | 185432 | |
| <I/σ(I)> | 12.7 | 5.7 |
| Completeness [%] | 95.3 | 82.8 |
| Redundancy | 3.6 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 293 | 50mM Tris, 1.9 M Ammonium sulfate, 3% PEG 400, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
