3TBF
C-terminal domain of glucosamine-fructose-6-phosphate aminotransferase from Francisella tularensis.
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 | 2011-07-03 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 71.370, 262.911, 83.797 |
| Unit cell angles | 90.00, 91.32, 90.00 |
Refinement procedure
| Resolution | 45.800 - 2.280 |
| R-factor | 0.1749 |
| Rwork | 0.172 |
| R-free | 0.23190 |
| Structure solution method | SAD |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.566 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHENIX |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 45.800 | 50.000 | 2.340 |
| High resolution limit [Å] | 2.280 | 6.240 | 2.280 |
| Rmerge | 0.061 | 0.021 | 0.429 |
| Number of reflections | 125776 | ||
| <I/σ(I)> | 10.1 | 2.11 | |
| Completeness [%] | 91.0 | 99.6 | 76.2 |
| Redundancy | 3.4 | 3.6 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 289 | 0.2 M trimethylamine N-oxide, 20% PEG MME 2000, 0.1 M Tris buffer, chymotrypsin, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
