8QTT
Crystal structure of a C-terminally truncated version of Arabidopsis thaliana 14-3-3 omega in complex with a phosphopeptide from the inhibitor protein BKI1.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-06-29 |
| Detector | DECTRIS PILATUS 2M-F |
| Wavelength(s) | 1.00003353518 |
| Spacegroup name | P 1 |
| Unit cell lengths | 71.216, 71.082, 150.986 |
| Unit cell angles | 100.47, 95.53, 88.74 |
Refinement procedure
| Resolution | 50.330 - 2.350 |
| R-factor | 0.2365 |
| Rwork | 0.234 |
| R-free | 0.27550 |
| Structure solution method | FOURIER SYNTHESIS |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.406 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.330 | 2.490 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmeas | 0.217 | 1.856 |
| Number of reflections | 118395 | 18838 |
| <I/σ(I)> | 5.5 | 0.95 |
| Completeness [%] | 98.1 | 96.5 |
| Redundancy | 3.7 | 3.7 |
| CC(1/2) | 1.000 | 0.510 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 12.5% w/v PEG 1000, 12.5% w/v PEG 3350, 12.5% v/v MPD, 0.02M of carboxylic acid, 0.1M MOPS/HEPES-Na pH7.5 |






