5A36
Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and incorporation in muscle.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I04 |
| Synchrotron site | Diamond |
| Beamline | I04 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-09-28 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 1 |
| Unit cell lengths | 38.658, 47.491, 70.299 |
| Unit cell angles | 80.78, 80.80, 76.50 |
Refinement procedure
| Resolution | 68.820 - 2.000 |
| R-factor | 0.21979 |
| Rwork | 0.217 |
| R-free | 0.26854 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.425 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 68.800 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.120 | 0.580 |
| Number of reflections | 31249 | |
| <I/σ(I)> | 5.8 | 1.5 |
| Completeness [%] | 96.0 | 82 |
| Redundancy | 2.2 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 30% POLYETHYLENE GLYCOL 1500, pH 7.5 |
