5GGP
Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-beta1,2-Man-peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-17A |
| Synchrotron site | Photon Factory |
| Beamline | BL-17A |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-12-21 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.9800 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 111.113, 49.743, 61.716 |
| Unit cell angles | 90.00, 105.89, 90.00 |
Refinement procedure
| Resolution | 46.554 - 1.599 |
| R-factor | 0.2176 |
| Rwork | 0.216 |
| R-free | 0.24640 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ggg |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.121 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.600 | 1.630 |
| High resolution limit [Å] | 1.599 | 1.600 |
| Rmerge | 0.103 | 0.729 |
| Number of reflections | 78168 | |
| <I/σ(I)> | 8.7 | 1.5 |
| Completeness [%] | 98.0 | 95.8 |
| Redundancy | 3.4 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | MES-NaOH, LiCl2, Na acetate, PEG-6000 |
