2Y9E
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 ID13 |
| Synchrotron site | ESRF |
| Beamline | ID13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-12-15 |
| Detector | ADSC 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 | 19.962 - 3.397 |
| R-factor | 0.2863 |
| Rwork | 0.282 |
| R-free | 0.37240 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mmd |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.447 |
| 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] | 20.000 | 3.660 |
| High resolution limit [Å] | 3.400 | 3.400 |
| Rmerge | 0.140 | 0.520 |
| Number of reflections | 15092 | |
| <I/σ(I)> | 7.34 | 2.44 |
| Completeness [%] | 99.7 | 99 |
| Redundancy | 8.7 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 100 MM HEPES (PH 7.5), 20% PEG10000 |
