5EA0
Structure of the antibody 7968 with human complement factor H-derived peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 93 |
| Detector technology | CCD |
| Collection date | 2014-12-05 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.280, 65.547, 71.267 |
| Unit cell angles | 90.00, 106.37, 90.00 |
Refinement procedure
| Resolution | 38.009 - 2.000 |
| R-factor | 0.2017 |
| Rwork | 0.196 |
| R-free | 0.27530 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1nl0 3QOS |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.256 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.030 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.059 | 0.421 |
| Number of reflections | 28263 | |
| <I/σ(I)> | 20.1 | 3.2 |
| Completeness [%] | 91.8 | 100 |
| Redundancy | 5 | 5.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 3.5 | 293 | Drop composed of Fab at 20 mg/ml mixed with 25 mM citric acid pH 3.5, 8% PEG 3350; over a reservoir of 24% PEG 3350 |
