3PMZ
Crystal Structure of the Complex of Acetylcholine Binding Protein and d-tubocurarine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-04-15 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 142.737, 194.042, 101.615 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 114.710 - 2.440 |
R-factor | 0.232 |
Rwork | 0.228 |
R-free | 0.29400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2byn |
RMSD bond length | 0.018 |
RMSD bond angle | 1.866 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 114.710 | 2.640 |
High resolution limit [Å] | 2.440 | 2.440 |
Rmerge | 0.109 | |
Number of reflections | 101910 | |
<I/σ(I)> | 41.3 | |
Completeness [%] | 96.9 | 93.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8 | 295 | 10% PEG 4000, 0.25M magnesium chloride, 0.1M Tris buffer pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K |