Azasulfurylpeptides feature an amino acid residue in which the CαH and the carbonyl are replaced respectively by a nitrogen atom and a sulfonyl group. Insight into the conformational preferences of azasulfurylpeptides containing an azasulfurylglycine (AsG) residue has been pursued using X‐ray analysis in the solid state. Crystals of N‐(Boc)‐Pro‐AsG‐Val‐OMe (10) and N‐(Cbz)‐Ala‐AsG‐D‐Phe‐Ot‐Bu (11) showed tetrahedral geometries about the sulfur atom with the ω torsion angle preferring a staggered conformation. Furthermore, the ϕ and ψ torsion angles of the central azasulfuryl residue were respectively within close proximity to those of ideal inverse and classical γ‐turns. In the crystal lattice, azasulfurylpeptide 11 engaged in intermolecular hydrogen bonds between the sulfonyl oxygen and hydrazide hydrogen in an antiparallel orientation. © 2015 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 104: 622–628, 2015.