4WIQ
The structure of Murine alpha-Dystroglycan T190M mutant N-terminal domain.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-05-09 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.0 |
| Spacegroup name | H 3 |
| Unit cell lengths | 71.879, 71.879, 144.296 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 48.099 - 1.590 |
| R-factor | 0.147 |
| Rwork | 0.146 |
| R-free | 0.16320 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1uc2 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.245 |
| Data reduction software | XDS (january 10, 2014) |
| Data scaling software | Aimless (0.2.17) |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.100 | 1.650 |
| High resolution limit [Å] | 1.590 | 1.590 |
| Rmerge | 0.045 | 0.442 |
| Number of reflections | 35504 | |
| <I/σ(I)> | 15.28 | 1.74 |
| Completeness [%] | 95.0 | 71.8 |
| Redundancy | 3.4 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | Protein solution: 5.25 mg/mL in 25 mM Tris, 150 mM NaCl and 2.5 % glycerol; pH 7.5 Precipitant solution: 0.8 M citrate buffer; pH 7.0 Drops volume: 1 microL protein solution + 1 microL precipitant solution Reservoir volume: 1 mL Crystals appeared after few days |






