4CBE
Crystal structure of complement factors H and FHL-1 binding protein BBH06 or CRASP-2 from Borrelia burgdorferi (Native)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-3 |
| Synchrotron site | MAX II |
| Beamline | I911-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-04-19 |
| Detector | MARMOSAIC 225 mm CCD |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 90.690, 48.840, 44.150 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 26.550 - 1.830 |
| R-factor | 0.19714 |
| Rwork | 0.195 |
| R-free | 0.23904 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4bg0 |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.841 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.220 | 1.870 |
| High resolution limit [Å] | 1.770 | 1.770 |
| Rmerge | 0.040 | 0.200 |
| Number of reflections | 19733 | |
| <I/σ(I)> | 17.8 | 6.1 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 3.6 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 0.2M SODIUM ACETATE, 0.1M TRIS PH 8.5, 30% PEG 2000MME |
