1UX2
X-ray structure of acetylcholine binding protein (AChBP)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-06-15 |
Detector | ADSC CCD |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 140.639, 140.639, 238.257 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 12.000 - 2.100 * |
R-factor | 0.23948 |
Rwork | 0.236 |
R-free | 0.28400 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1i9b |
RMSD bond length | 0.012 * |
RMSD bond angle | 1.320 * |
Data reduction software | MOSFLM |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.111 | 0.932 |
Number of reflections | 236373 | |
<I/σ(I)> | 10 | 1.3 |
Completeness [%] | 99.0 | 99 |
Redundancy | 13.4 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 | TRIS PH 8.0, AMMONIUM SULFATE |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium sulfate | 1.4 (M) | |
2 | 1 | reservoir | PEG200 | 1 (%) | |
3 | 1 | reservoir | HEPES | 0.1 (M) | pH7.0 |
4 | 1 | drop | Tris | 0.1 (M) | pH8.0 |