6R1G
Crystal structure of Borrelia burgdorferi periplasmic protein BB0365 (IPLA7, p22)
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 | 2017-01-21 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.94934 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 50.650, 63.470, 61.210 |
| Unit cell angles | 90.00, 111.34, 90.00 |
Refinement procedure
| Resolution | 47.220 - 1.550 |
| R-factor | 0.1761 |
| Rwork | 0.175 |
| R-free | 0.19160 |
| Structure solution method | SAD |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.936 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | SHELXCD |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.220 | 1.630 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.039 | 0.288 |
| Number of reflections | 50688 | 7281 |
| <I/σ(I)> | 18.9 | 4.8 |
| Completeness [%] | 96.9 | 95.6 |
| Redundancy | 6.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 294 | 0.2 M Na acetate 0.1 M Tris pH 8.5 35% PEG 550 |
