2Y0R
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 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 54.600, 106.000, 178.900 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.980 - 2.850 |
| R-factor | 0.2558 |
| Rwork | 0.253 |
| R-free | 0.30110 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mmd |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.572 |
| 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] | 91.290 | 2.920 |
| High resolution limit [Å] | 2.850 | 2.850 |
| Rmerge | 0.180 | 0.460 |
| Number of reflections | 23285 | |
| <I/σ(I)> | 8.53 | 2.61 |
| Completeness [%] | 97.9 | 77.2 |
| Redundancy | 4.5 | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 100 MM MES (PH 6.5), 25% PEG 8000. |
