cover illustration The red fluorescent protein DsRed was engineered from an obligate tetramer into a monomer by a combination of targeted and random mutagenesis. This monomeric variant, called DsRed.M1, crystallizes in space group P212121 with a single molecule in the asymmetric unit. Analysis of the crystal packing reveals that the polar (magenta) and hydrophobic (green) tetramerization interfaces of wild-type DsRed are completely disrupted in DsRed.M1. Sidechains of the former tetramerization interface residues are indicated, and the chromophore is shown in CPK. For details, please see Strongin et al., pp. 525-534.
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