5OMA
CH3 chimera of human 14-3-3 sigma with the StARD1 peptide including Ser57
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04 |
Synchrotron site | Diamond |
Beamline | I04 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-06-20 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 0.9282 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 123.251, 123.251, 162.447 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.000 - 3.900 |
R-factor | 0.212 |
Rwork | 0.209 |
R-free | 0.24800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5LU1 (monomer) |
RMSD bond length | 0.010 |
RMSD bond angle | 1.110 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | BUSTER (2.10.3) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 47.000 | 47.000 | 4.130 |
High resolution limit [Å] | 3.890 | 11.390 | 3.890 |
Rmerge | 0.265 | 0.057 | 2.885 |
Rmeas | 0.277 | 0.060 | 3.006 |
Number of reflections | 12047 | 553 | 1870 |
<I/σ(I)> | 6.88 | 34.84 | 0.97 |
Completeness [%] | 99.7 | 97 | 99.2 |
Redundancy | 12.71 | 10.837 | 12.658 |
CC(1/2) | 0.998 | 0.998 | 0.214 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1 M bis-Trispropane pH 6.5, 0.2 M ammonium sulfate, 25% PEG 3350 |