5A37
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 | 2012-12-16 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 1 |
| Unit cell lengths | 38.240, 46.490, 70.380 |
| Unit cell angles | 73.68, 80.08, 75.53 |
Refinement procedure
| Resolution | 67.140 - 1.880 |
| R-factor | 0.17979 |
| Rwork | 0.178 |
| R-free | 0.21586 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.147 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.600 | 1.980 |
| High resolution limit [Å] | 1.900 | 1.880 |
| Rmerge | 0.080 | 0.410 |
| Number of reflections | 34585 | |
| <I/σ(I)> | 7.6 | 2 |
| Completeness [%] | 94.2 | 91.1 |
| Redundancy | 2.1 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 28% POLYETHYLENE GLYCOL 2000, pH 7.5 |
