2CH5
Crystal structure of human N-acetylglucosamine kinase in complex with N-acetylglucosamine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-04-19 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 |
| Unit cell lengths | 57.537, 98.482, 101.981 |
| Unit cell angles | 63.43, 75.66, 75.06 |
Refinement procedure
| Resolution | 90.170 - 1.900 |
| R-factor | 0.167 |
| Rwork | 0.167 |
| R-free | 0.19900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | HUMAN N-ACETYLGLUCOSAMINE KINASE IN COMPLEX WITH ADP AND GLUCOSE |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.361 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 2.050 | 2.050 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.050 | 0.320 |
| Number of reflections | 140534 | |
| <I/σ(I)> | 16.8 | 2.5 |
| Completeness [%] | 93.3 | 81.2 |
| Redundancy | 1.7 | 1.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.6 | 100 MM HEPES PH 7.0, 100 MM NACL, 8% (W/V) PEG 4000, 2MM GLCNAC |
