5GGO
Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GalNac-beta1,3-GlcNAc-beta-pNP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL15A1 |
| Synchrotron site | NSRRC |
| Beamline | BL15A1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-08-05 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 70.016, 89.705, 53.358 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 27.827 - 1.502 |
| R-factor | 0.1764 |
| Rwork | 0.175 |
| R-free | 0.20810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ggg |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.628 |
| 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] | 45.900 | 1.500 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.085 | 0.901 |
| Number of reflections | 54584 | |
| <I/σ(I)> | 14.7 | 2.1 |
| Completeness [%] | 100.0 | 99.9 |
| Redundancy | 7.2 | 7.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.8 | 293 | Tris-HCl, PEG-6000 |
