1VZJ
Structure of the tetramerization domain of acetylcholinesterase: four-fold interaction of a WWW motif with a left-handed polyproline helix
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4A |
Synchrotron site | NSLS |
Beamline | X4A |
Temperature [K] | 100 |
Collection date | 2001-04-15 |
Wavelength(s) | 0.96672,0.97927,0.97895,1.5415 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 53.730, 58.790, 58.800 |
Unit cell angles | 90.00, 111.38, 90.00 |
Refinement procedure
Resolution | 40.000 - 2.350 |
R-factor | 0.247 |
Rwork | 0.247 |
R-free | 0.25900 |
Structure solution method | MAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.202 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE/RESOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.000 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.054 | 0.349 |
Number of reflections | 12935 | |
<I/σ(I)> | 11.1 | 1.47 |
Completeness [%] | 89.4 | 58.5 |
Redundancy | 2.7 | 1.75 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.6 | 10% ISOPROPANOL, 10% PEG, 4K 0.05 M TRISODIUM CITRATE, PH 5.6 |