5U56
Structure of Francisella tularensis heterodimeric SspA (MglA-SspA)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.1 |
| Synchrotron site | ALS |
| Beamline | 5.0.1 |
| Temperature [K] | 80 |
| Detector technology | CCD |
| Collection date | 2016-10-15 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9774 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 66.408, 113.261, 140.400 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.077 - 2.650 |
| R-factor | 0.2073 |
| Rwork | 0.204 |
| R-free | 0.25870 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4pur 1yy7 |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.565 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.700 |
| High resolution limit [Å] | 2.650 | 2.650 |
| Rmerge | 0.076 | 0.784 |
| Number of reflections | 31478 | |
| <I/σ(I)> | 31.74 | 2.13 |
| Completeness [%] | 99.9 | 99.7 |
| Redundancy | 7.2 | 6.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | PEGRX2 17 L-proline, HEPES, PEG 1500 |
