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The X-ray crystal structure of Thermus aquaticus core RNA polymerase reveals a ''crab claw''-shaped molecule with a 27 Å wide internal channel. Located on the back wall of the channel is a Mg 2+ ion required for catalytic activity, which is chelated by an absolutely conserved motif from all bacterial and eukaryotic cellular RNA polymerases. The structure places key functional sites, defined...
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