4ARB
Mus musculus Acetylcholinesterase in complex with (S)-C5685 at 2.25 A resolution.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I911-3 |
Synchrotron site | MAX II |
Beamline | I911-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-01-29 |
Detector | MARMOSAIC 225 mm CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 78.926, 111.781, 227.071 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.806 - 2.250 |
R-factor | 0.1722 |
Rwork | 0.172 |
R-free | 0.20910 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1j06 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.090 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | REFMAC |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.100 | 2.370 |
High resolution limit [Å] | 2.250 | 2.250 |
Rmerge | 0.070 | 0.480 |
Number of reflections | 96077 | |
<I/σ(I)> | 16 | 3.7 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 5.7 | 5.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | 0.1 M HEPES, 30 % (V/V) POLYETHELENEGLYCOLEMONOMETHYLETHER, pH 7 |