4N39
Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26)
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 315r |
| Wavelength(s) | 1.075 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 101.170, 101.170, 131.730 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 33.116 - 1.760 |
| R-factor | 0.1887 |
| Rwork | 0.187 |
| R-free | 0.21580 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.899 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA (3.3.16) |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 87.616 | 33.116 | 1.860 |
| High resolution limit [Å] | 1.760 | 5.570 | 1.760 |
| Rmerge | 0.044 | 0.628 | |
| Total number of observations | 12104 | 58259 | |
| Number of reflections | 77414 | ||
| <I/σ(I)> | 9.1 | 14 | 1.1 |
| Completeness [%] | 99.6 | 92.3 | 100 |
| Redundancy | 5.1 | 4.9 | 5.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 1.5 M Potassium Sodium Tartrate, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
