6MA2
Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor ent-1a
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-06-23 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 98.610, 98.610, 365.111 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 85.399 - 2.100 |
| R-factor | 0.187 |
| Rwork | 0.185 |
| R-free | 0.21800 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 4n3a |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.808 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless (0.5.12) |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 91.280 | 91.280 | 2.150 |
| High resolution limit [Å] | 2.100 | 9.390 | 2.100 |
| Rmerge | 0.190 | 0.079 | 1.230 |
| Rmeas | 0.203 | 0.085 | 1.335 |
| Rpim | 0.072 | 0.032 | 0.511 |
| Total number of observations | 483344 | ||
| Number of reflections | 62582 | 890 | 4499 |
| <I/σ(I)> | 6.2 | ||
| Completeness [%] | 100.0 | 100 | 99.8 |
| Redundancy | 7.7 | 6.6 | 6.6 |
| CC(1/2) | 0.992 | 0.994 | 0.571 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 1.05 M Sodium Citrate Tribasic Dihydrate, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
