5A4B
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 I02 |
| Synchrotron site | Diamond |
| Beamline | I02 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-01-31 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 1 |
| Unit cell lengths | 38.390, 46.630, 69.860 |
| Unit cell angles | 73.80, 80.02, 75.05 |
Refinement procedure
| Resolution | 66.680 - 2.010 |
| R-factor | 0.19943 |
| Rwork | 0.198 |
| R-free | 0.23464 |
| Structure solution method | OTHER |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.408 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0123) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 66.680 | 2.060 |
| High resolution limit [Å] | 2.010 | 2.010 |
| Rmerge | 0.090 | 0.250 |
| Number of reflections | 28251 | |
| <I/σ(I)> | 6.2 | 2.2 |
| Completeness [%] | 95.0 | 95.1 |
| Redundancy | 2.1 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 24% POLYETHYLENE GLYCOL 3350, pH 7.5 |
