2GYV
Crystal structure of Mus musculus Acetylcholinesterase in complex with Ortho-7
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I711 |
Synchrotron site | MAX II |
Beamline | I711 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-02-02 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.131 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 76.730, 108.580, 220.580 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.000 - 2.500 |
R-factor | 0.198 |
Rwork | 0.197 |
R-free | 0.24100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1j06 |
RMSD bond length | 0.014 |
RMSD bond angle | 1.545 |
Data scaling software | XDS |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.000 | 2.640 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.086 | 0.507 |
Number of reflections | 64151 | |
<I/σ(I)> | 19.6 | 4.8 |
Completeness [%] | 99.4 | 99.1 |
Redundancy | 7.5 | 7.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 278 | 26-30 % PEG750MME, 0.1 M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 278K |