5GZ9
Crystal structure of catalytic domain of Protein O-mannosyl Kinase in complexes with AMP-PNP, Magnesium ions and glycopeptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-07-24 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 81.320, 81.320, 146.838 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 40.192 - 2.400 |
| R-factor | 0.2338 |
| Rwork | 0.232 |
| R-free | 0.26840 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5gz8 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.171 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 2.440 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.742 | |
| Number of reflections | 249333 | |
| <I/σ(I)> | 20.7 | 3.3 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 11 | 11 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 0.1M Tris-HCl (pH 8.5), 23% (w/v) PEG 3350 |
