Balch, William
is interested in the biochemical and molecular basis for vesicular trafficking from the endoplasmic reticulum to the cell surface, particularly in the structures, functions, and mechanisms of control exerted by small GTP-binding proteins.
Carragher, Bridget O.
is developing, testing, and applying technology for specimen handling, automated acquisition, automated processing, and information handling in electron microscopy; one of the goals is to completely automate cryo-electron microscopy in order to solve macromolecular structures.
Cline, Hollis
studies the analysis of the activity-dependent control of cell proliferation, neuronal development and circuit formation in the visual system using gene transfer, in vivo imaging and electrophysiological techniques.
Franc, Nathalie C
studies phagocytosis, the process by which dying cells are recognized and cleared during embryogenesis in the fruit fly, Drosophila melanogaster. Her long-term goal is to compare its molecular mechanisms with that of phagocytosis of pathogens, such as bacteria.
Johnson Jr., John Emil
uses a variety of cellular and molecular biology methods to develop and test atomic resolution models of particle-related events in the virus life cycle; he also uses viruses as a paradigm for developing methods to determine atomic resolution models of cellular mega-structures.
MacRae, Ian John
combines structural biology, biochemistry and cell biology to understand mechanisms of gene regulation by RNA interference.
Milligan, Ronald A.
uses cryo-electron microscopy and image analysis to study the structure and mechanism of action of large molecular machines such as actomyosin, kinesin-microtubules, MAPs-microtubles, VCP/p97 and dynein AAA ATPases, various membrane channels and transporters, and bacterial toxins.
Mueller, Ulrich
focuses on the genes and the gene mutations that contribute to the pathology of Usher syndrome, other human diseases related to mechanosensory perception, and central nervous system diseases
Potter, Clinton S.
is developing, testing, and applying technology for specimen handling, automated acquisition, automated processing, and information handling in electron microscopy; one of the goals is to completely automate cryo-electron microscopy in order to solve macromolecular structures.
Stevens, Raymond C.
uses crystallography and biochemistry to probe the structure and function of molecules involved in neurotransmission and neurochemistry, seeking to understand how neuronal cells communicate at the molecular level and to create new molecules that affect neuronal signal transduction and recognition.
Stout, C. D.
determines crystal structures of a variety of biological macromolecules, primarily integral membrane associated enzymes and proton pumps, cytochrome P450s, and iron-sulfur enzymes, and including HIV protease mutants, self-assembling peptides, and RNA-protein complexes, in order to understand structure-function relationships and establish mechanism.
Tainer, John A.
develops and applies advanced tools for high-impact structural biology including combined x-ray scattering in solution and x-ray crystallography on complexes at his synchrotron beamline to bridge
from complexes and conformations to pathways and phenotypes by characterizing macromolecular machines, novel inhibitors, and the molecular basis for diseases and intervention strategies.
Yeager, Mark J.
uses high resolution electron cryo-microscopy and image analysis to explore the architecture of supramolecular assemblies, such as transmembrane signaling proteins and channels (integrins, gap junction channels, and aquaporins) and viruses responsible for significant human disease (rotaviruses, astroviruses, and retroviruses).
