5M7T
Structure of human O-GlcNAc hydrolase with PugNAc type inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I02 |
| Synchrotron site | Diamond |
| Beamline | I02 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-08-01 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 101.146, 101.146, 283.289 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 95.440 - 2.600 |
| R-factor | 0.2037 |
| Rwork | 0.203 |
| R-free | 0.23510 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.545 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 95.440 | 2.690 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.092 | 2.279 |
| Rpim | 0.026 | 0.634 |
| Number of reflections | 46333 | |
| <I/σ(I)> | 16.1 | 1.1 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 13.2 | 13.7 |
| CC(1/2) | 0.590 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 292 | 0.1-0.2 M tri Ammonium citrate 16-20 % PEG 3350 |
