8FE7
Crystal structure of human O-GlcNAc transferase (OGT) in complex with an exosite-binding peptide (SMG9) and UDP-GlcNAc
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2020-09-17 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 3 2 1 |
| Unit cell lengths | 273.669, 273.669, 143.144 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 118.500 - 2.980 |
| R-factor | 0.1867 |
| Rwork | 0.186 |
| R-free | 0.21740 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.600 |
| 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] | 237.000 | 3.030 |
| High resolution limit [Å] | 2.980 | 2.980 |
| Number of reflections | 125036 | 6187 |
| <I/σ(I)> | 13.7 | |
| Completeness [%] | 99.5 | |
| Redundancy | 7.7 | |
| CC(1/2) | 0.998 | 0.784 |
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 |
