ATOMIC RESOLUTION STUDIES OF FERREDOXIN FROM HALOARCULA MARISMORTUI

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The research in my lab has focused on the structure determination of (i) bacterial channel-forming toxins, such as Staphylococcal leukocidin (LukF) and (ii) the ligand binding domain of ligand gated ion channels. Data from the F2 beamline has enabled us to solve the structure of the water-soluble form of LukF and the ligand binding domain of the GluR2, AMPA-selective glutamate receptor. Both structures were solved by MAD phasing from selenomethionine crystals at ~2.3 A resolution. Presently, both structures have been refined and we are currently in the process of manuscript preparation. From these structures we have furthered our understanding, at the molecular level, of the conformational changes that bacterial toxins undergo as a consequence of membrane binding and oligomerization and we have provided, for the first time, a view of the extracellular domain of a ligand gated ion channel.