8QT5
Crystal structure of Arabidopsis thaliana 14-3-3 isoform lambda in complex with a phosphopeptide from the transcription factor BZR1.
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 | 2017-05-13 |
Detector | DECTRIS PILATUS 2M-F |
Wavelength(s) | 1.03320713866 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 176.052, 176.052, 172.031 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 74.920 - 2.690 |
R-factor | 0.2417 |
Rwork | 0.241 |
R-free | 0.26160 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.002 |
RMSD bond angle | 0.406 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 74.920 | 2.850 |
High resolution limit [Å] | 2.690 | 2.690 |
Rmeas | 0.111 | 3.037 |
Number of reflections | 84698 | 13110 |
<I/σ(I)> | 19.54 | 1.09 |
Completeness [%] | 98.5 | 95.2 |
Redundancy | 20.2 | 20.8 |
CC(1/2) | 1.000 | 0.536 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | 22 % [w/v] PEG 10,000, 0.1 M ammonium acetate, 0.1 M Bis-Tris [pH 5.5] |