The cover shows the crystal structure of a cold-active alpha-amylase from a bacterium collected along the antarctic ice shell where water temperature never exceeds 2|0C. It exhibits the (B/a)8 barrel structure typical of all a-amylases from family 13 glycoside hydrases. Compared with mesophilic homologues, this enzyme has lost several weak interactions in order to acquire the required conformational plasticity for catalysis at low temperatures. For details see the article by D'Amico et al., pages 25791-25796.25791.