Extended Data Fig. 1: Synthesis and crystal structure of ZnGGH-1⋅(DMF-H2O).
From: Chemical control of structure and guest uptake by a conformationally mobile porous material
a, Schematic representation of ZnGGH-1⋅(DMF-H2O) synthesis from glycine–glycine–l-histidine and Zn(OAc)2. The tripeptide is deprotonated at the C-terminal acid and the imidazole side chain. The resulting anion acts as a tetratopic linker and coordinates to four Zn2+ cations, thus forming a three-dimensional (4,4)-connected net. b, Top, structural representation of ZnGGH-1⋅(DMF-H2O) viewed along the b axis reveals the parallelogram-shaped one-dimensional pores. Centre, the rigid layers of the framework are composed of the histidine residue. Each histidine links three Zn2+ cations; two of them are bridged by the imidazolate side chain, and the third is bound to the carboxylate group. Bottom, ZnGGH-1⋅(DMF-H2O) viewed along the a axis shows the undulating shape of the rigid layers, which are interconnected by the flexible glycine–glycine chains.
