8CRA
Structure of the keratin-like domain of SEPALLATA3 and AGAMOUS from Arabidopsis thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-11-10 |
Detector | DECTRIS PILATUS 2M |
Wavelength(s) | 0.873 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 101.335, 138.372, 180.229 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.400 |
R-factor | 0.2388 |
Rwork | 0.237 |
R-free | 0.27911 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.331 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | REFMAC |
Refinement software | REFMAC (5.8.0405) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 82.000 | 2.450 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmeas | 0.097 | 1.630 |
Number of reflections | 95018 | 6627 |
<I/σ(I)> | 11.3 | 0.9 |
Completeness [%] | 99.3 | 0.932 |
Redundancy | 3.8 | |
CC(1/2) | 0.999 | 0.347 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 277 | 0.1M Tris, pH 8.0, 2M sodium formate |