2XUD
Crystal structure of the Y337A mutant of mouse acetylcholinesterase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-11-10 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 79.424, 109.015, 227.839 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.650 |
| R-factor | 0.19407 |
| Rwork | 0.193 |
| R-free | 0.22768 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1j06 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.393 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALA |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.720 |
| High resolution limit [Å] | 2.650 | 2.650 |
| Rmerge | 0.080 | 0.410 |
| Number of reflections | 57806 | |
| <I/σ(I)> | 12.5 | 4 |
| Completeness [%] | 99.1 | 99.1 |
| Redundancy | 3.5 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | PROTEIN WAS CRYSTALLIZED FROM PEG-600 25-35% (V/V) IN 50-100 MM HEPES, PH 6.0-7.0, OR WITH PEG-550 MME 30% (V/V) IN 50 MM NA ACETATE, PH 7.5 |
