5DTI
Crystal structure of mouse acetylcholinesterase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-10-30 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.075 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 78.411, 113.135, 227.199 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.999 - 2.003 |
R-factor | 0.1974 |
Rwork | 0.197 |
R-free | 0.22380 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ha2 |
RMSD bond length | 0.005 |
RMSD bond angle | 0.981 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | PHENIX (1.9_1685) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.000 |
Number of reflections | 126503 |
<I/σ(I)> | 27.8 |
Completeness [%] | 93.0 |
Redundancy | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 274 | 30% v/v PEG 600, 0.1 M sodium citrate |