6VLG
Crystal structure of mouse alpha 1,6-fucosyltransferase, FUT8 bound to GDP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-11-03 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9536 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 150.820, 150.820, 472.139 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 49.367 - 2.500 |
| R-factor | 0.1844 |
| Rwork | 0.182 |
| R-free | 0.22730 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2de0 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.16_3549) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.370 | 2.540 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.157 | 0.713 |
| Rmeas | 0.164 | 0.772 |
| Rpim | 0.049 | 0.279 |
| Total number of observations | 1135283 | 28905 |
| Number of reflections | 109145 | 4637 |
| <I/σ(I)> | 9.5 | 2 |
| Completeness [%] | 98.8 | 85.8 |
| Redundancy | 10.4 | 6.2 |
| CC(1/2) | 0.995 | 0.811 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 298 | 12% PEG 3350, 0.25 M NH4SO4, 0.1 M Tris, pH 7.4 |
