Post-Doctoral Position: Structure-Function of Membrane Proteins; Cytochrome b6f Complex of Oxygenic Photosynthesis
The group of W. A. Cramer at Purdue University is seeking an outstanding Post-Doctoral researcher to extend the understanding of the structure and function of the cytochrome b6f complex in oxygenic photosynthesis. We have obtained a 2.5 A structure of the
250 kDa hetero-oligomeric complex (pdb 4OGQ) using continuous beam synchrotron radiation, conducted at the nearby (200 km) Argonne National Laboratory, which has provided major insight into structure-function. Because the b6f complex controls the
rate-limiting step in the linear electron transport chain, future structure studies will focus on the mechanism of rate limitation, pathways of proton transfer involving lipophilic quinone(ol) and quinone-analogue inhibitors in the linear and cyclic electron transfer chains, and the interaction of the complex with peripheral proteins including the trans-membrane chlorophyll protein kinase, and would continue the use X-ray diffraction analysis, and utilize Cryo-EM as well with the Titan microscope that is in-house. Candidates should have demonstrated expertise in the biochemistry, expression, and purification of membrane proteins and macromolecular structure analysis. Interested individuals should contact W. A. Cramer at email@example.com.