Crystal and Structural Chemistry
Bijvoet Centre for Biomolecular Research
Department of Chemistry, Faculty of Science
There is currently one 2.5-year ERC-funded post-doctoral positions available on structural, biophysical and biochemical studies of the human complement system.
Please send applications (consisting of a CV, a motivation letter and two references) to firstname.lastname@example.org.
Ternary complex C3b-FH-FI reveals molecular mechanisms underlying Cofactor Activity and complement-immune processing
Heterogeneous MAC initiator and pore structures in a lipid bilayer by phase-plate cryo-electron tomography
Regulators of complement activity mediate inhibitory mechanisms through common C3b-binding mode
Structures of Wnt-antagonist ZNRF3 and its complex with R-spondin 1 and implications for signaling
Density maps at 10-Å resolution for the whole C1-IgG16 complex and 7-Å resolution for the hexameric gC1q-Fc platform
Substrate C3 is superposed on the S. aureus SCIN inhibited C3 convertase C3bBb dimer.
Morph showing the changes between the structures of C3 and C3b.
Coloured by domain
Disease related mutations mapped onto the structure of C3b-FH(1-4).