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 |