2Q1S
Crystal structure of the Bordetella bronchiseptica enzyme WbmF in complex with NADH
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 | 83.186, 77.875, 59.411 |
| Unit cell angles | 90.00, 108.19, 90.00 |
Refinement procedure
| Resolution | 38.520 - 1.500 |
| R-factor | 0.19358 |
| Rwork | 0.192 |
| R-free | 0.22622 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ENTRIES 1BXK 1keu 1r6d |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.617 |
| 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 | 1.530 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.052 | 0.658 |
| Number of reflections | 57271 | |
| <I/σ(I)> | 29.5 | 1.83 |
| Completeness [%] | 99.3 | 94.8 |
| Redundancy | 4.8 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9 | 293 | 0.1 M bicine, 16 % (w/w) PEG 8000, pH 9, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
