6ROC
Crystal structure of Borrelia burgdorferi outer surface protein BBA69, mutant Leu214Met (Se-Met data)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-01-24 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.9797 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 73.970, 110.552, 61.695 |
| Unit cell angles | 90.00, 126.83, 90.00 |
Refinement procedure
| Resolution | 52.190 - 2.900 |
| R-factor | 0.2021 |
| Rwork | 0.199 |
| R-free | 0.26710 |
| Structure solution method | SAD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.503 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | SHELXCD |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 52.190 | 3.080 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.063 | 0.225 |
| Number of reflections | 8521 | 1374 |
| <I/σ(I)> | 13.2 | 5.6 |
| Completeness [%] | 96.7 | 95.9 |
| Redundancy | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 294 | 0.1M (NH4)2SO4 0.1M Tris pH 8.0 25% PEG 3350 |
