2I0Z
Crystal structure of a FAD binding protein from Bacillus cereus, a putative NAD(FAD)-utilizing dehydrogenases
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-03-06 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.98400 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 46.716, 92.366, 97.504 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.860 - 1.840 |
| R-factor | 0.19779 |
| Rwork | 0.195 |
| R-free | 0.24794 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2gqf |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.329 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 1.920 |
| High resolution limit [Å] | 1.840 | 1.840 |
| Rmerge | 0.075 | 0.394 |
| Number of reflections | 36967 | |
| <I/σ(I)> | 13.9 | 3.9 |
| Completeness [%] | 98.9 | 99.7 |
| Redundancy | 3.9 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.3 | 295 | 0.01M TRIS-HCL, 0.2M Ammonium chloride, 0.25M Sodium chloride, 20% PEG 3350, pH 8.3, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
