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 |