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Front cover: The three-dimensional view of a bacterial protein histidine phosphatase SixA reveals a compact alpha/beta architecture related to RHG phosphatases for small substrates. Compared with these RHG phosphatases, SixA lacks an extra helical domain to form an open active site for the substrate protein. The extra domains in phosphoglycerate mutase (brown), fructose-2,6-bisphosphatase (blue) and acid phosphatase (red) cover their active sites. For details, see the article by Hamada et al. (pp. 1-11) in this issue.