4F21
Crystal structure of carboxylesterase/phospholipase family protein from Francisella tularensis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-11-21 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 |
| Unit cell lengths | 50.997, 64.416, 139.039 |
| Unit cell angles | 94.89, 90.12, 89.96 |
Refinement procedure
| Resolution | 29.458 - 2.500 |
| R-factor | 0.204 |
| Rwork | 0.199 |
| R-free | 0.25850 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fj2 |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.802 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.540 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.078 | 0.360 |
| Number of reflections | 58087 | |
| <I/σ(I)> | 8.4 | 2.2 |
| Completeness [%] | 94.4 | 97.5 |
| Redundancy | 1.9 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 0.1 M ammonium acetate, 0.1 M Bis-Tris, 17% PEG10000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
