5BJV
X-ray structure of the PglF UDP-N-acetylglucosamine 4,6-dehydratase from Campylobacterjejuni, D396N/K397A variant in complex with UDP-N-acrtylglucosamine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-09-01 |
| Detector | Bruker Platinum 135 |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 69.820, 108.468, 108.959 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.800 |
| R-factor | 0.19419 |
| Rwork | 0.192 |
| R-free | 0.23167 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5bju |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.895 |
| Data reduction software | SAINT |
| Data scaling software | SADABS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0124) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.095 | 0.310 |
| Number of reflections | 74633 | 10235 |
| <I/σ(I)> | 7.7 | 2 |
| Completeness [%] | 96.4 | 89.3 |
| Redundancy | 4.2 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | 13% PEG-5000, 10 mM UDP, 100 mM MES, |
