3PND
FAD binding by ApbE protein from Salmonella enterica: a new class of FAD binding proteins
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-1 |
| Synchrotron site | SSRL |
| Beamline | BL9-1 |
| Temperature [K] | 75 |
| Detector technology | IMAGE PLATE |
| Collection date | 2008-12-11 |
| Detector | MAR scanner 345 mm plate |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 65.103, 120.850, 212.058 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.600 - 2.750 |
| R-factor | 0.205 |
| Rwork | 0.202 |
| R-free | 0.25440 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2o18 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.899 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.2.25) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 32.600 | 32.599 | 2.820 |
| High resolution limit [Å] | 2.750 | 12.300 | 2.750 |
| Rmerge | 0.093 | 0.033 | 0.400 |
| Total number of observations | 2009 | 13860 | |
| Number of reflections | 44268 | ||
| <I/σ(I)> | 14.7 | 12 | 1.9 |
| Completeness [%] | 99.7 | 91.6 | 99.9 |
| Redundancy | 4.2 | 3.8 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 8.5 | 277 | 0.5M LiSO4, 18% polyethylene glycol (PEG) 4000 in 100 mM Tris-HCl, and 10-20 mg/ml as purified FAD bound ApbE, pH 8.5, VAPOR DIFFUSION, temperature 277K |






