6BYK
Structure of 14-3-3 beta/alpha bound to O-ClcNAc 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 | 2016-07-16 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 82.670, 71.450, 95.759 |
| Unit cell angles | 90.00, 111.61, 90.00 |
Refinement procedure
| Resolution | 89.030 - 3.000 |
| R-factor | 0.2199 |
| Rwork | 0.215 |
| R-free | 0.26830 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4dnk |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.729 |
| 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] | 89.030 | 3.160 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rpim | 0.063 | 0.359 |
| Number of reflections | 36435 | |
| <I/σ(I)> | 9 | 2.1 |
| Completeness [%] | 95.7 | 97.9 |
| Redundancy | 3 | 2.5 |
| CC(1/2) | 0.995 | 0.786 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | 30% PEG 4000, 200 mM sodium acetate, 0.1 M Tris pH 8.5 |
