3MYH
Insights into the Importance of Hydrogen Bonding in the Gamma-Phosphate Binding Pocket of Myosin: Structural and Functional Studies of Ser236
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 32-ID |
| Synchrotron site | APS |
| Beamline | 32-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-11-20 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.97885 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 88.430, 146.440, 153.760 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.620 - 2.010 |
| R-factor | 0.19147 |
| Rwork | 0.189 |
| R-free | 0.23958 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vom |
| RMSD bond length | 0.024 |
| RMSD bond angle | 1.980 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0066) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.620 | 2.080 |
| High resolution limit [Å] | 2.000 | 2.010 |
| Rmerge | 0.061 | 0.237 |
| Number of reflections | 64281 | |
| <I/σ(I)> | 18.6 | 2.9 |
| Completeness [%] | 96.7 | 90.1 |
| Redundancy | 5.2 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | 12% PEG8K, 250mM MgCl2, 100mM MOPS, 2mM ADP, 3mM sodium vanadate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
