Structures of the Grb2 SH2 domain complexed with a series of flexible and constrained replacements of the phosphotyrosine residue in tripeptides derived from Ac-pYXN (where X = V, I, E and Q) were compared to determine what, if any, structural differences arise as a result of ligand preorganization.

The preparation and structural investigation of seven solvates of the anti­hypertensive drug olmesartan are described. All the structures were found to be isostructural and the supra­molecular arrangements are held in a similar way by strong N—HO hydrogen bonds.