In collaboration with Julie Sando, Anesthesiology U.VA., we have determined the low resolution, three dimensional structure of protein kinase C  from two dimensional crystals grown on phospholipid monolayers by electron microscopy. We are exploring the occurrence and functions of tandemly repeated sequences whose structures are inherently flexible. We are evaluating the placements of amino acid side chains in protein structures, determined by homology modeling. We are analyzing the concerted changes in conformation that accompany the binding of calcium by proteins in the EF-hand homolog family.

Shumilin, I.A., Bauerle, R., Wu, J., Woodard, R.W., and Kretsinger, R. H. "Crystal structure of the reaction complex of 3-deoxy-D-arabino-heptulosonate-7-phosphate Synthase from Thermotoga maritima Refines the Catalytic Mechanism and Indicates a New Mechanism of Allosteric Regulation" J. Mol. Biol. (2004) 341 455-466.

Kretsinger, R.H. "Proteins and the Flow of Information in Cellular Function" in Molecular Imaging: FRET Microscopy and Spectroscopy pp 1 - 15 eds. A. Perisasamy and R.N. Day Oxford University Press (2005).

Solodukhin, A.S., Kretsinger, R.H. and Sando, J.J. "Initial three-dimensional Reconstructions of Protein Kinase C delta from two-dimensional Crystals on Lipid Monolayers" Cellular Signalling (2007) 19 2033-2045.