Riboswitches are non-coding RNA sequences that control cellular processes through ligand binding. Conformational heterogeneity is fundamental to riboswitch functionality, yet this same attribute makes structural characterization of these mRNA elements challenging. Here, we use cryo-electron microscopy to characterize different structural populations of the glycine riboswitch tandem aptamers, and molecular dynamics simulations to support the observed ligand orientation in the holo state. We find that Mg
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A 1959 study studied this question.