3U8J
Crystal structure of the acetylcholine binding protein (AChBP) from Lymnaea stagnalis in complex with NS3531 (1-(pyridin-3-yl)-1,4-diazepane)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-01-01 |
| Detector | ADSC QUANTUM 210 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 72.350, 114.430, 247.370 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.880 - 2.350 |
| R-factor | 0.206 |
| Rwork | 0.205 |
| R-free | 0.25800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1UW6: PENTAMER CHAIN A-E |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.010 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.3.9) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.6.4_486) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.880 | 2.480 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmerge | 0.083 | 0.268 |
| Number of reflections | 83502 | |
| <I/σ(I)> | 9.1 | 2.9 |
| Completeness [%] | 97.1 | 88.6 |
| Redundancy | 3 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 293 | 50mM Tris, 1.9M Ammonium sulfate, 1% PEG 400, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
