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The first crystal structure of a proteorhodopsin shows a hexametric ring of protein in which the conserved photoactive-site histidine forms a hydrogen bond to the Schiff base proton acceptor from the same molecule and also to a tryptophan residue of a neighboring protomer. The structure and mutant studies reveal novel aspects of the ion translocation mechanism and cooperative behavior between protomers involving the inter-molecular His-Trp pair.

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X-ray crystallographic structures of four p53 core-domain variants were determined in order to gain insights into the mechanisms by which certain second-site suppressor mutations rescue the function of a significant number of cancer mutations of the tumor suppressor protein p53.
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