3PE4
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 X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-11-15 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.000 |
Spacegroup name | I 1 2 1 |
Unit cell lengths | 98.600, 136.700, 153.500 |
Unit cell angles | 90.00, 102.90, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.950 |
R-factor | 0.2254 |
Rwork | 0.224 |
R-free | 0.25180 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.050 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.6.1_357)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.060 |
High resolution limit [Å] | 1.950 | 1.950 |
Number of reflections | 141571 | |
<I/σ(I)> | 8.4 | 4.7 |
Completeness [%] | 98.4 | 94.5 |
Redundancy | 3.1 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 1.6M Lithium Sulfate, 0.1M Bis Tris Propane pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |