2YHW
High-resolution crystal structures of N-Acetylmannosamine kinase: Insights about substrate specificity, activity and inhibitor modelling.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARMOSAIC 225 mm CCD |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 90.730, 90.730, 100.780 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.370 - 1.640 |
| R-factor | 0.14933 |
| Rwork | 0.148 |
| R-free | 0.17019 |
| Structure solution method | OTHER |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.026 |
| RMSD bond angle | 2.068 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 45.300 |
| High resolution limit [Å] | 1.640 |
| Rmerge | 0.060 |
| Number of reflections | 52083 |
| <I/σ(I)> | 30.66 |
| Completeness [%] | 100.0 |
| Redundancy | 12.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 0.2 M CALCIUM ACETATE, 0.1 M SODIUM CACODYLATE PH 6.5 AND 40% PEG 300. |
