8FUF
Crystal structure of human O-GlcNAc transferase (OGT) in complex with an exosite-binding peptide (ZNF831) and UDP-GlcNAc
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2020-11-08 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.12717 |
Spacegroup name | P 3 2 1 |
Unit cell lengths | 274.011, 274.011, 143.078 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 53.060 - 3.690 |
R-factor | 0.1989 |
Rwork | 0.198 |
R-free | 0.24160 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.002 |
RMSD bond angle | 0.445 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 137.010 | 3.750 |
High resolution limit [Å] | 3.690 | 3.690 |
Number of reflections | 66589 | 3338 |
<I/σ(I)> | 12.1 | 2.2 |
Completeness [%] | 99.9 | |
Redundancy | 20.7 | |
CC(1/2) | 0.997 | 0.768 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 1.9M Ammonium Sulfate, 0.1M Tris pH=8.5, 1% Xylitol |