Biphenyl degradation by recombinant photosynthetic cyanobacterium Synechocystis sp. PCC6803 in an oligotrophic environment using unphysiological electron transfer
Non-conservation of folding rates in the thioredoxin family reveals degradation of ancestral unassisted-folding
In this issue Qu and colleagues (pp. 3649–3660) have determined the crystal structure of TauA and have characterized its thermodynamic binding parameters by isothermal titration calorimetry in complex with taurine and different alkanesulfonates. The cover figure shows desolvation of the taurine binding protein TauA dictates ligand selectivity. TauA is shown in cartoon with taurine in red sticks. Water droplets indicate fully hydrated binding site. Image provided by Konstantinos Beis.