3PE3
Structure of human O-GlcNAc transferase and its complex with a peptide substrate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-09-08 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0809 |
Spacegroup name | P 3 2 1 |
Unit cell lengths | 273.400, 273.400, 142.800 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 48.583 - 2.780 |
R-factor | 0.1852 |
Rwork | 0.185 |
R-free | 0.21770 |
Structure solution method | MIR |
RMSD bond length | 0.003 |
RMSD bond angle | 0.707 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | SHARP |
Refinement software | PHENIX ((phenix.refine: 1.6.1_357)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.930 |
High resolution limit [Å] | 2.780 | 2.780 |
Number of reflections | 154231 | |
<I/σ(I)> | 8.4 | 3 |
Completeness [%] | 98.2 | 95.1 |
Redundancy | 3.3 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 1.45 M Potassium Phosphate Dibasic, 8 mM EDTA, 1% xylitol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |