5N4H
Crystal structure of the D109N mutant of the mouse alpha-Dystroglycan N-terminal region
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-03-10 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 1.000 |
| Spacegroup name | H 3 |
| Unit cell lengths | 71.740, 71.740, 143.990 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 47.997 - 1.701 |
| R-factor | 0.1603 |
| Rwork | 0.159 |
| R-free | 0.18240 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1u2c |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.270 |
| Data reduction software | XDS (VERSION OCT 15, 2015) |
| Data scaling software | XSCALE (VERSION OCT 15, 2015) |
| Phasing software | PHASER (2.7.2) |
| Refinement software | PHENIX ((1.11_2561)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.096 | 1.098 |
| Rmeas | 0.103 | 1.181 |
| Number of reflections | 30354 | 2776 |
| <I/σ(I)> | 11.96 | 1.96 |
| Completeness [%] | 99.7 | 97.9 |
| Redundancy | 7.8 | 7.5 |
| CC(1/2) | 0.997 | 0.833 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | 0.7 M Citrate Buffer, pH 7.0 5.5 mg/mL protein in 25 mM Tris, 150 mM NaCl, pH 7.5 |






