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Bacteria are remarkable at tailoring their bioenergetic machineries to adapt to and thrive in diverse and ever-changing environments. A critical metabolic task is the efficient extraction of energy from food. Similar to us, many bacteria pass electrons to oxygen or other acceptors with the help of membrane-bound enzymes, and in doing so, they move protons across their membrane, thus generating a transmembrane voltage (much like a battery) that can be used for ATP synthesis. Typically, one enzyme passes an electron to its downstream enzyme via random collisions. However, sometimes these enzymes can form a supercomplex that positions the enzymes very close to each other and with the right pose for faster electron transfer and therefore more efficient energy conversion. In a recent paper reporting a three-way collaboration between biochemists, experimental structural biologists, and the Center researchers, the structure of one such supercomplex (termed Alternative complex III) was determined at an atomic resolution through a combination of cryoEM and advanced molecular modeling and simulation tools performed with NAMD and VMD. Read more about this study in Nature.