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 |






