5OK9
CH1 chimera of human 14-3-3 sigma with the HSPB6 phosphopeptide in a conformation with swapped phosphopeptides
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I02 |
Synchrotron site | Diamond |
Beamline | I02 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-02-02 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 0.9795 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 63.631, 140.635, 68.663 |
Unit cell angles | 90.00, 114.75, 90.00 |
Refinement procedure
Resolution | 46.650 - 2.350 |
R-factor | 0.193 |
Rwork | 0.191 |
R-free | 0.24000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5lu1 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.040 |
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] | 46.650 | 46.650 | 2.350 |
High resolution limit [Å] | 2.210 | 6.580 | 2.210 |
Rmerge | 0.229 | 0.073 | 1.795 |
Rmeas | 0.266 | 0.085 | 2.095 |
Total number of observations | 186114 | ||
Number of reflections | 48345 | 2071 | 4536 |
<I/σ(I)> | 5.51 | 16.84 | 0.73 |
Completeness [%] | 88.3 | 97 | 51.5 |
Redundancy | 3.85 | 3.765 | 3.645 |
CC(1/2) | 0.984 | 0.994 | 0.285 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1 M MMT (malateMES-Tris) buffer (pH 4) and 25% PEG 1500 |