5I5K
Structure of complement C5 in complex with eculizumab
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-11-17 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.97625 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 197.704, 269.321, 202.824 |
Unit cell angles | 90.00, 98.58, 90.00 |
Refinement procedure
Resolution | 49.795 - 4.200 |
R-factor | 0.2055 |
Rwork | 0.204 |
R-free | 0.24360 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4kmt 3pvm |
RMSD bond length | 0.003 |
RMSD bond angle | 0.641 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10_2152: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.800 | |
High resolution limit [Å] | 4.200 | 4.200 |
Number of reflections | 76073 | |
<I/σ(I)> | 6.28 | 1.29 |
Completeness [%] | 99.6 | 99.9 |
Redundancy | 4.9 | 5.01 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 277.15 | 0.1 M Imidazole pH 6.2 4% v/v Tacsimate pH 7 8% PEG 3350 |