5GGL
Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-alpha-pNP
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 | 2014-11-10 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.9800 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 53.330, 68.686, 88.136 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.124 - 1.270 |
| R-factor | 0.1451 |
| Rwork | 0.145 |
| R-free | 0.16060 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ggg |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.284 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.100 | 1.290 |
| High resolution limit [Å] | 1.270 | 1.270 |
| Rmerge | 0.090 | 1.840 |
| Number of reflections | 86073 | |
| <I/σ(I)> | 14.4 | 1.3 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 12.7 | 12.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.8 | 293 | Tris-HCl, PEG-8000 |
