6VLF
Crystal structure of mouse alpha 1,6-fucosyltransferase, FUT8 in its Apo-form
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 | 2018-08-25 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9537 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 184.874, 71.353, 126.951 |
| Unit cell angles | 90.00, 126.08, 90.00 |
Refinement procedure
| Resolution | 44.527 - 1.800 |
| R-factor | 0.1854 |
| Rwork | 0.184 |
| R-free | 0.20820 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2de0 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.2) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.16_3549) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.200 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.052 | 1.268 |
| Rmeas | 0.062 | 1.496 |
| Rpim | 0.033 | 0.788 |
| Total number of observations | 422751 | 21511 |
| Number of reflections | 123197 | 6122 |
| <I/σ(I)> | 10.6 | 0.9 |
| Completeness [%] | 99.6 | 99.7 |
| Redundancy | 3.4 | 3.5 |
| CC(1/2) | 0.999 | 0.463 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 298 | 12% PEG 3350, 0.25 M NH4SO4, 0.1M Tris, pH 7.4 |
