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The article discusses research which evaluates the manno-oligosaccharide-binding ability of mouse ReglV/GST-fusion protein by complex formation with the carbohydrate-containing polyamidoamine dendrimer (PD). It noted that GST-mReglV showed affinity for mannan- and manno-oligosaccharide containing PD. It informs that binding was inhibited by manno-oligosaccharides but not by mannose which reveals extended structure of binding site in contrast with carbohydrate-binding protein lectins.

No crystal structures are yet available for homologues of a predicted acetamidase/formamidase (Amds/Fmds) from the arch aeon Thermoanaero- bacter tengcongensis. The Amds/Fmds gene was cloned and expressed as a soluble protein in Escherichia coli. Native Amds/Fmds and its SeMet-substituted form were purified and crystallized by vapour diffusion in hanging drops at 296 K. The native crystals, which were grown in PEG 8000, belong to the monoclinic space group P21, with unit-cell parameters a = 41.23 (3), b = 152.88 (6), c = 100.26 (7) Å, β = 99.49 (3)°. The diffraction data were collected to 2.00 Å resolution using synchrotron radiation. Based on a predicted solvent content of 50%, a Matthews coefficient of 2.44 ų Da-1 and two main peaks in the self-rotation function, the asymmetric unit is predicted to contain two dimers of the 32 kDa native protein. MAD data were collected for the SeMet protein, but the corresponding crystals display different unit-cell parameters and appear to contain four dimers in the asymmetric unit. [ABSTRACT FROM AUTHOR]