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Rodney Burton got his BS and PhD in Biochemistry at the University of Illinois, Urbana-Champaign on the biophysical internal mechanisms of electron transport proteins. He then went on to do two Postdoctoral fellowships at Michigan State University, Lansing, and the University of Michigan, Ann Arbor. He has also done research on the mechanisms of phosphoglycerate dehydrogenase enzyme from the bacteria causing tuberculosis and leprosy. Other disease-focused research includes viruses, immune system receptors, and malaria.

He lives in ɫ��ӰƬ as a proud husband and father of four. Scholarship and Research: Worshiping God through excellence in science, integrity, and teamwork is our mission as we investigate the assembly and bioengineering of the vault shell protein complex. This large hollow complex is found in almost all eukaryotic cells, however still has no known function after decades of study, however its presence is elevated in cancer cells. We are developing methods for improved growth and assembly of the vault proteins and proteins that associate with them, in the hopes of bioengineering better solutions for drug delivery and cancer treatment.

However, our primary goal in lab is developing students as disciples of Christ with habits of treating lab members with dignity and respect, being good stewards of the lab space, and of reporting the truth with clarity.

Select Publications & Presentations:

• A. R. Hagen et al., In vitro assembly of diverse bacterial microcompartment shell architectures. Nano letters 18, 7030-7037 (2018).   
• M. C. Rodney Burton, Daniel Esckilsen, Seth Wiley and Stephen W. Ragsdale, in Enzymes of Energy Technology. (2018), vol. 613.   
• A. R. Crofts et al., The Q-cycle mechanism of the bc 1 complex: a biologist’s perspective on atomistic studies. The Journal of Physical Chemistry B 121, 3701-3717 (2017).   
• E. J. Young et al., Engineering the bacterial microcompartment domain for molecular scaffolding applications. Frontiers in microbiology 8, 1441 (2017).   
• R. L. Burton, S. Chen, X. L. Xu, G. A. Grant, Role of the anion-binding site in catalysis and regulation of Mycobacterium tuberculosis D-3phosphoglycerate dehydrogenase. Biochemistry 48, 4808-4815 (2009). S. Dey, R. L. Burton, G. A. Grant, J. C. Sacchettini, Structural analysis of substrate and effector binding in Mycobacterium tuberculosis D-3phosphoglycerate

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