2Q1T
Crystal structure of the Bordetella bronchiseptica enzyme WbmF in complex with NAD+ and UDP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-05-18 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.977 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 83.442, 78.119, 59.262 |
| Unit cell angles | 90.00, 108.08, 90.00 |
Refinement procedure
| Resolution | 28.520 - 1.750 |
| R-factor | 0.18302 |
| Rwork | 0.183 |
| R-free | 0.21900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ENTRIES 1BXK 1keu 1r6d |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.746 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.780 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.049 | 0.337 |
| Number of reflections | 33895 | |
| <I/σ(I)> | 23.7 | 2.38 |
| Completeness [%] | 93.3 | 62.6 |
| Redundancy | 3.9 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9 | 293 | 0.1 M bicine, 16 % (w/w) PEG 8000. UDP was added by soaking prior to cryo-protection., pH 9, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
