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 |