2Q1U
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 | 121.851, 79.682, 84.953 |
| Unit cell angles | 90.00, 113.10, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.700 |
| R-factor | 0.17736 |
| Rwork | 0.177 |
| R-free | 0.21100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | The starting model was the related PDB entry 2PZJ the same protein in a different crystal form. The biological unit (i.e. a dimer) generated from crystallographic symmetry was used as the search model. |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.538 |
| 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 | 1.730 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.055 | 0.459 |
| Number of reflections | 81311 | |
| <I/σ(I)> | 21.9 | 2.18 |
| Completeness [%] | 98.4 | 87.1 |
| Redundancy | 3.9 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 0.1 M Tris, 0.2 M calcium acetate, 20 % (w/v) PEG 3000, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
