4BDT
Human acetylcholinesterase in complex with huprine W and fasciculin 2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-06-19 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | H 3 2 |
Unit cell lengths | 151.600, 151.600, 246.400 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 57.934 - 3.104 |
R-factor | 0.1621 |
Rwork | 0.159 |
R-free | 0.21890 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2x8b |
RMSD bond length | 0.008 |
RMSD bond angle | 1.291 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 58.000 | 3.200 |
High resolution limit [Å] | 3.100 | 3.100 |
Rmerge | 0.090 | 0.660 |
Number of reflections | 19677 | |
<I/σ(I)> | 16 | 3 |
Completeness [%] | 98.1 | 93.7 |
Redundancy | 3.1 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.4 | 0.1 M HEPES BUFFER PH 7.4, 1.3 M AMMONIUM SULFATE |