6BYL
Structure of 14-3-3 gamma bound to O-GlcNAcylated thr peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-03-26 |
Detector | ADSC QUANTUM 210r |
Wavelength(s) | 1.0 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 121.200, 121.200, 310.900 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 112.923 - 3.350 |
R-factor | 0.237 |
Rwork | 0.234 |
R-free | 0.28480 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5USK |
RMSD bond length | 0.003 |
RMSD bond angle | 0.466 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 112.923 | 3.530 |
High resolution limit [Å] | 3.350 | 3.350 |
Rmeas | 0.115 | 1.003 |
Rpim | 0.068 | 0.613 |
Number of reflections | 32119 | 4440 |
<I/σ(I)> | 6.2 | 1.2 |
Completeness [%] | 94.5 | 91.5 |
Redundancy | 2.3 | 2.2 |
CC(1/2) | 0.997 | 0.530 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | 29% PEG 4000, 200 mM sodium acetate, 0.1 M Tris pH 8.5 |