5A38
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 | 38.300, 46.560, 70.160 |
Unit cell angles | 73.81, 80.26, 75.38 |
Refinement procedure
Resolution | 67.000 - 1.900 |
R-factor | 0.19377 |
Rwork | 0.192 |
R-free | 0.23088 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1wku |
RMSD bond length | 0.009 |
RMSD bond angle | 1.324 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.650 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.070 | 0.390 |
Number of reflections | 33050 | |
<I/σ(I)> | 7.2 | 2.1 |
Completeness [%] | 94.0 | 94 |
Redundancy | 1.9 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 22% POLYETHYLENE GLYCOL 3350, pH 7.5 |