5N30
Crystal structure of the V72I 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) | 0.9763 |
Spacegroup name | H 3 |
Unit cell lengths | 71.810, 71.810, 143.990 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 35.905 - 1.800 |
R-factor | 0.1555 |
Rwork | 0.154 |
R-free | 0.18240 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1u2c |
RMSD bond length | 0.016 |
RMSD bond angle | 1.338 |
Data reduction software | XDS (VERSION Oct 15, 2015) |
Data scaling software | XSCALE (VERSION Oct 15, 2015 BUILT=20151231) |
Phasing software | PHASER (2.7.2) |
Refinement software | PHENIX ((1.11_2561: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 36.000 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.105 | 1.306 |
Rmeas | 0.106 | 1.362 |
Number of reflections | 25641 | 2530 |
<I/σ(I)> | 15.84 | 2.13 |
Completeness [%] | 99.9 | 99.4 |
Redundancy | 11.5 | 11.3 |
CC(1/2) | 0.999 | 0.862 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 277 | Cross streak-Seeding (from D109N alpha-DG mutant) 1 muL protein solution + 1 muL precipitant Seeding after 3-6 days of equilibration Protein Solution: (5 mg / mL protein, 25 mM Tris, 150 mM NaCl, pH 7.5) Precipitant: 0.8 M citrate buffer, pH 7.2 |