4BG0
Crystal structure of complement factors H and FHL-1 binding protein BBH06 or CRASP-2 from Borrelia burgdorferi
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 | 2013-02-01 |
| Detector | MARMOSAIC 225 mm CCD |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 90.480, 48.890, 44.310 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.230 - 2.100 |
| R-factor | 0.19173 |
| Rwork | 0.190 |
| R-free | 0.22610 |
| Structure solution method | SAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.435 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SHELX |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.800 | 2.210 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.040 | 0.170 |
| Number of reflections | 12042 | |
| <I/σ(I)> | 15.4 | 5.7 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 13.8 | 13.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 0.2M SODIUM ACETATE, 0.1M TRIS PH 8.5, 30% PEG 2000MME |
