4OKO
Crystal structure of Francisella tularensis REP34 (Rapid Encystment Phenotype Protein 34 KDa)
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 | 2012-12-16 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.2837 |
| Spacegroup name | P 1 |
| Unit cell lengths | 62.712, 63.308, 81.689 |
| Unit cell angles | 70.36, 84.34, 82.53 |
Refinement procedure
| Resolution | 21.535 - 2.053 |
| R-factor | 0.2134 |
| Rwork | 0.213 |
| R-free | 0.23250 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | SAD SE-MET SOLUTION FOR ZN-FREE CRYSTAL |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.849 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SOLVE |
| Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 22.000 | 2.090 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.103 | 0.579 |
| Number of reflections | 68959 | |
| <I/σ(I)> | 8.98 | 2.07 |
| Completeness [%] | 94.9 | 83.1 |
| Redundancy | 2.6 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 298 | 20% w/v PEG4000, 0.1 M sodium acetate, pH 4.7-5.3, VAPOR DIFFUSION, HANGING DROP, temperature 298K |






