4GYW
Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide
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 | 2011-04-29 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.075 |
Spacegroup name | I 1 2 1 |
Unit cell lengths | 99.000, 137.770, 153.566 |
Unit cell angles | 90.00, 102.90, 90.00 |
Refinement procedure
Resolution | 43.904 - 1.700 |
R-factor | 0.1881 |
Rwork | 0.187 |
R-free | 0.20500 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 0.972 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | PHENIX (1.7_650) |
Refinement software | PHENIX ((phenix.refine: 1.7_650)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.904 | 1.790 |
High resolution limit [Å] | 1.700 | 1.700 |
Number of reflections | 206769 | |
Completeness [%] | 94.3 | 87.1 |
Redundancy | 3.2 |
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 |