5KOE
The structure of Arabidopsis thaliana FUT1 in complex with XXLG
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | BRUKER AXS MICROSTAR |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-10-13 |
| Detector | Bruker Platinum 135 |
| Wavelength(s) | 1.54188 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 81.748, 80.150, 157.616 |
| Unit cell angles | 90.00, 91.91, 90.00 |
Refinement procedure
| Resolution | 157.530 - 1.790 |
| R-factor | 0.16811 |
| Rwork | 0.166 |
| R-free | 0.21676 |
| Structure solution method | SAD |
| RMSD bond length | 0.024 |
| RMSD bond angle | 2.085 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.890 |
| High resolution limit [Å] | 1.790 | 1.790 |
| Rmerge | 0.095 | 0.723 |
| Number of reflections | 191803 | |
| <I/σ(I)> | 11.61 | 1.48 |
| Completeness [%] | 99.8 | 98.8 |
| Redundancy | 7.75 | 5.32 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 7 mg/mL protein in 0.1 M MES pH 6.0 to 7.0 and 16% to 23% w/v PEG 3350 |
