6X5U
Human Alpha-1,6-fucosyltransferase (FUT8) bound to GDP and NM5M2-Asn
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 | 2020-03-01 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.00 |
Spacegroup name | P 65 |
Unit cell lengths | 154.020, 154.020, 466.920 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 87.840 - 3.200 |
R-factor | 0.1943 |
Rwork | 0.190 |
R-free | 0.23590 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6x5h |
RMSD bond length | 0.002 |
RMSD bond angle | 0.550 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.13_2998) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 87.842 | 3.280 |
High resolution limit [Å] | 3.200 | 3.200 |
Rmeas | 0.259 | 1.400 |
Number of reflections | 102079 | 7647 |
<I/σ(I)> | 5.7 | 1.2 |
Completeness [%] | 99.3 | 99.9 |
Redundancy | 3.6 | 3.7 |
CC(1/2) | 0.985 | 0.509 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 10% PEG 3350, 0.2 M Ammonium chloride |