2Y8I
Structural basis for the allosteric interference of myosin function by mutants G680A and G680V of Dictyostelium myosin-2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-01-28 |
| Detector | MARMOSAIC 225 mm CCD |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 55.000, 105.800, 180.500 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.215 - 3.132 |
| R-factor | 0.2494 |
| Rwork | 0.245 |
| R-free | 0.33650 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mmd |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.360 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | AMoRE |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.220 | 3.190 |
| High resolution limit [Å] | 3.130 | 3.130 |
| Rmerge | 0.170 | 0.460 |
| Number of reflections | 20093 | |
| <I/σ(I)> | 9.23 | 2.37 |
| Completeness [%] | 96.4 | 83.4 |
| Redundancy | 11.1 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 13% PEG 6000, 4% GLYCEROL., pH 7.0 |
