8SFW
Crystal structure of TuUGT202A2 (Tetur22g00270) in complex with quercetin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-04-13 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0000 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 45.884, 109.420, 165.840 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.916 - 2.750 |
Rwork | 0.207 |
R-free | 0.26410 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.474 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0405) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.800 |
High resolution limit [Å] | 2.750 | 2.750 |
Rmeas | 0.209 | 0.629 |
Rpim | 0.086 | 0.258 |
Number of reflections | 10446 | 434 |
<I/σ(I)> | 11.8 | 1.9 |
Completeness [%] | 92.0 | 79.9 |
Redundancy | 5.7 | 5.4 |
CC(1/2) | 0.960 | 0.886 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | Quercetin dissolved in ETOH and let it evaporate on plate. Protein incubated with UDP. 0.2 M Ammonium acetate 0.1 M BIS-TRIS pH 6.5 25% w/v Polyethylene glycol 3,350 |