6BYJ
Structure of human 14-3-3 gamma bound to O-GlcNAc 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 | 2016-07-15 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 122.270, 122.270, 314.100 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 113.942 - 2.900 |
| R-factor | 0.2293 |
| Rwork | 0.228 |
| R-free | 0.26920 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3uzd |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.544 |
| 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] | 113.942 | 3.060 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.067 | |
| Rpim | 0.022 | 0.305 |
| Number of reflections | 53876 | 7734 |
| <I/σ(I)> | 18.6 | 2.5 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 8.8 | 7 |
| CC(1/2) | 0.999 | 0.768 |
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 |
