3DOA
The crystal structure of the fibrinogen binding protein from Staphylococcus aureus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-03-27 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9794 |
| Spacegroup name | I 41 2 2 |
| Unit cell lengths | 102.269, 102.269, 166.911 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 87.040 - 2.810 |
| R-factor | 0.1908 |
| Rwork | 0.187 |
| R-free | 0.27048 |
| Structure solution method | SAD |
| RMSD bond length | 0.026 |
| RMSD bond angle | 2.282 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MLPHARE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 87.040 | 2.880 |
| High resolution limit [Å] | 2.810 | 2.810 |
| Number of reflections | 10541 | |
| <I/σ(I)> | 21.84 | 1.7 |
| Completeness [%] | 98.9 | 88.09 |
| Redundancy | 16.9 | 9.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | 10% PEG4000, 45% tacsimate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
