8XWG
OspA variants for thioflavin-T binding
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-5A |
| Synchrotron site | Photon Factory |
| Beamline | BL-5A |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-12-18 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 1.00000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.183, 35.807, 92.397 |
| Unit cell angles | 90.00, 105.99, 90.00 |
Refinement procedure
| Resolution | 19.660 - 2.000 |
| R-factor | 0.2345 |
| Rwork | 0.232 |
| R-free | 0.28050 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.865 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.660 | 2.071 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.116 | 0.692 |
| Number of reflections | 22435 | 1831 |
| <I/σ(I)> | 8.98 | 1.55 |
| Completeness [%] | 97.2 | 80.48 |
| Redundancy | 3.3 | 2.6 |
| CC(1/2) | 0.997 | 0.740 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.25 | 293 | 42%(w/v) PEG400, 0.1 M Tris-HCl, 15 mg/mL protein |
