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 |
R-factor | 0.23093 |
Rwork | 0.231 |
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] | 999.000 | 2.279 |
High resolution limit [Å] | 1.530 | 2.200 |
Rmeas | 0.185 | 0.864 |
Number of reflections | 101962 | 10549 |
<I/σ(I)> | 7.41 | |
Completeness [%] | 88.3 | |
Redundancy | 2 | |
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 |