8SFT
Crystal structure of TuUGT202A2 (Tetur22g00270) in complex with kaempferol
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 | 2022-03-13 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 83.277, 159.906, 163.311 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.588 - 2.750 |
| Rwork | 0.192 |
| R-free | 0.23160 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.518 |
| 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 | 2.820 |
| High resolution limit [Å] | 2.750 | 2.750 |
| Rmeas | 0.183 | 0.846 |
| Rpim | 0.072 | 0.313 |
| Number of reflections | 56602 | 2850 |
| <I/σ(I)> | 14 | 2.1 |
| Completeness [%] | 95.7 | 98.4 |
| Redundancy | 6.2 | 6.6 |
| CC(1/2) | 0.985 | 0.829 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | Protein incubated with 1 mM UDP and kaempferol dissolved in ethanol. 0.2 M Ammonium sulfate 0.1 M HEPES pH 7.5 25% PEG 3350 |
