8P22
X-ray structure of acetylcholine-binding protein (AChBP) in complex with IOTA376.
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | MAX IV BEAMLINE BioMAX |
| Synchrotron site | MAX IV |
| Beamline | BioMAX |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-04-04 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9762 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 143.960, 120.600, 133.160 |
| Unit cell angles | 90.00, 91.50, 90.00 |
Refinement procedure
| Resolution | 49.510 - 2.200 |
| Rwork | 0.238 |
| R-free | 0.30380 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.702 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0419) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.510 | 2.279 |
| High resolution limit [Å] | 1.530 | 2.200 |
| Rmerge | 0.138 | 0.654 |
| Rmeas | 0.185 | 0.864 |
| Number of reflections | 101963 | 10549 |
| <I/σ(I)> | 7.41 | 1.12 |
| Completeness [%] | 88.3 | 91.57 |
| Redundancy | 2 | 1.9 |
| CC(1/2) | 0.907 | 0.588 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | PEG 3350 3% Ammonium sulphate 1.8M HEPES buffer 0.1M, pH 7.75 |
