4BL4
Further structural insights into the binding of complement factor H by complement regulator acquiring surface protein 1, CspA (BbCRASP-1), of Borrelia burgdorferi.
Replaces: 4ATRExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 120 |
| Detector technology | CCD |
| Collection date | 2009-11-21 |
| Detector | MARRESEARCH |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 115.370, 44.160, 186.540 |
| Unit cell angles | 90.00, 90.69, 90.00 |
Refinement procedure
| Resolution | 93.260 - 4.060 |
| R-factor | 0.2629 |
| Rwork | 0.262 |
| R-free | 0.27070 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1w33 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.100 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.11.4) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 93.260 | 4.160 |
| High resolution limit [Å] | 4.060 | 4.060 |
| Rmerge | 0.190 | 0.600 |
| Number of reflections | 7629 | |
| <I/σ(I)> | 5.7 | 2.7 |
| Completeness [%] | 95.9 | 98.6 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 18% (W/V) PEG 8000, 5MM ZINC ACETATE, 100MM SODIUM CACODYLATE, PH 6.5 |
