8FE6
Crystal structure of human O-GlcNAc transferase (OGT) in complex with an exosite-binding peptide 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 | 2020-10-14 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.127129 |
Spacegroup name | H 3 |
Unit cell lengths | 281.532, 281.532, 143.212 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 40.640 - 3.060 |
R-factor | 0.1816 |
Rwork | 0.181 |
R-free | 0.21940 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.003 |
RMSD bond angle | 0.532 |
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] | 123.485 | 3.113 |
High resolution limit [Å] | 3.060 | 3.060 |
Number of reflections | 79618 | 3990 |
<I/σ(I)> | 12.9 | |
Completeness [%] | 99.7 | |
Redundancy | 10.5 | |
CC(1/2) | 0.994 | 0.492 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 1.45M potassium phosphate, 10mM EDTA pH 8, 1% Xylitol |