4GZ3
Crystal structure of human O-GlcNAc Transferase with UDP and a thioglycopeptide
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 | 2011-07-19 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.075 |
Spacegroup name | I 1 2 1 |
Unit cell lengths | 98.770, 137.620, 153.016 |
Unit cell angles | 90.00, 102.82, 90.00 |
Refinement procedure
Resolution | 48.154 - 1.900 |
R-factor | 0.2274 |
Rwork | 0.226 |
R-free | 0.24960 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 0.915 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | PHENIX (1.7.2_869) |
Refinement software | PHENIX ((phenix.refine: 1.7.2_869)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.870 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Number of reflections | 154828 | |
Completeness [%] | 99.1 | 99 |
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 |