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Structural analysis of six potassium salts of hypodiphospho­ric acid, H4P2O6, containing the anions in all possible basicities, is focused on the anion structure and the organization of the anionic and cationic sublattices.

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Cocrystallization of baicalein with nicotinamide yields a 1:1 cocrystal [systematic name: pyridine-3-carboxamide-5,6,7-trihy­droxy-2-phenyl-4H-chromen-4-one (1/1)], C6H6N2O·C15H10O5. The asymmetric unit contains one baicalein and one nicotinamide mol­ecule, both in neutral forms. Mol­ecules in the cocrystal form column motifs stabilized by an array of inter­molecular hydrogen bonds.

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In the crystal structure of the L-His-cIMP complex, i.e. L-histidinium inosine 3':5'-cyclic phosphate [systematic name: 5-(2-amino-2-carb­oxy­eth­yl)-1H-imidazol-3-ium 7-hy­droxy-2-oxo-6-(6-oxo-6,9-dihydro-1H-purin-9-yl)-4a,6,7,7a-tetra­hydro-4H-1,3,5,2[lambda]5-furo[3,2-d][1,3,2[lambda]5]dioxaphosphinin-2-olate], C6H10N3O2+·C10H10N4O7P-, the Hoogsteen edge of the hypo­xanthine (Hyp) base of cIMP and the Hyp face are engaged in specific amino acid-nucleotide (His...cIMP) recognition, i.e. by abutting edge-to-edge and by [pi]-[pi] stacking, respectively. The Watson-Crick edge of Hyp and the cIMP phosphate group play a role in nonspecific His...cIMP contacts. The inter­actions between the cIMP anions (anti/C3'-endo/trans-gauche/chair conformers) are realized mainly between riboses and phosphate groups. The results for this L-His-cIMP complex, compared with those for the previously reported solvated L-His-IMP crystal structure, indicate a different nature of amino acid-nucleotide recognition and inter­actions upon the 3':5'-cyclization of the nucleotide phosphate group.
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