4N3A
Crystal Structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (1-26)E10A
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 | 2011-10-11 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.1 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 98.929, 98.929, 367.015 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 45.858 - 1.880 |
| R-factor | 0.2015 |
| Rwork | 0.200 |
| R-free | 0.22220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.062 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA (3.3.20) |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.7.3_928) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 85.675 | 45.858 | 1.980 |
| High resolution limit [Å] | 1.880 | 5.950 | 1.880 |
| Rmerge | 0.053 | 0.599 | |
| Total number of observations | 22853 | 46145 | |
| Number of reflections | 82602 | ||
| <I/σ(I)> | 7.3 | 12.2 | 1.1 |
| Completeness [%] | 95.0 | 93.6 | 96.1 |
| Redundancy | 3.8 | 7.9 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 0.72M Potassium Phosphate Monobasic, 0.88M Potassium Phosphate Dibasic, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
