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 |