5KWK
The structure of Arabidopsis thaliana FUT1 in complex with GDP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | BRUKER AXS MICROSTAR |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-11-10 |
| Detector | Bruker Platinum 135 |
| Wavelength(s) | 1.54188 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.933, 113.103, 87.781 |
| Unit cell angles | 90.00, 105.01, 90.00 |
Refinement procedure
| Resolution | 84.780 - 1.900 |
| R-factor | 0.22583 |
| Rwork | 0.223 |
| R-free | 0.28882 |
| RMSD bond length | 0.025 |
| RMSD bond angle | 2.175 |
| Data reduction software | PROTEUM PLUS |
| Data scaling software | PROTEUM PLUS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 84.780 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.134 | 0.590 |
| Number of reflections | 79818 | |
| <I/σ(I)> | 6.3 | 1.5 |
| Completeness [%] | 99.8 | 99.7 |
| Redundancy | 5.11 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 7 mg/mL protein in 0.1 M MES pH 6.0 to 7.0 and 16% to 23% w/v PEG 3350 |
