4ZK4
Crystal structure of a chimeric acetylcholine binding protein from Aplysia californica (Ac-AChBP) containing loop C from the human alpha 3 nicotinic acetylcholine receptor in complex with 7-(5-isopropoxy-pyridin-3-yl)-1-methyl-1,7-diaza-spiro[4.4]nonane
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.2 |
Synchrotron site | ALS |
Beamline | 8.2.2 |
Temperature [K] | 88 |
Detector technology | CCD |
Collection date | 2011-12-20 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.999 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 70.662, 78.205, 120.465 |
Unit cell angles | 90.00, 94.97, 90.00 |
Refinement procedure
Resolution | 49.135 - 1.901 |
R-factor | 0.1826 |
Rwork | 0.181 |
R-free | 0.21250 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB entries 2BYN 2byp 2byr 2bys 2pgz 3c79 3c84 |
RMSD bond length | 0.014 |
RMSD bond angle | 1.318 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.880 |
High resolution limit [Å] | 1.850 | 5.020 | 1.850 |
Rmerge | 0.086 | 0.044 | 0.584 |
Total number of observations | 812969 | ||
Number of reflections | 110948 | ||
<I/σ(I)> | 13.9 | ||
Completeness [%] | 99.7 | 99.9 | 95.9 |
Redundancy | 7.3 | 7.4 | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | 1.7% PEG400, 0.085 M HEPES sodium, pH 7.5, 1.7 M ammonium sulfate, 15% glycerol |