Exploring humidity effects on polycrystalline human insulin-ligand complexes: preliminary crystallographic insights.

ABSTRACT: This study investigates the effect of relative humidity (RH) on the crystal structures of human insulin (HI) complexes with organic ligands, m-cresol and m-nitro-phenol, using in situX-ray powder diffraction (XRPD) with a controlled-humidity chamber. Co-crystallization at pH 7.5 produced hexagonal microcrystals (space group R3) for both protein-ligand complexes. The corresponding single-crystal X-ray diffraction structures were solved: HI-m-cresol (PDB entry 9ibb, 1.84 Å) and HI-m-nitro-phenol (PDB entry 9qld, 2.55 Å). Pawley analysis of the in situ XRPD data revealed structural stability up to 70% RH, with no phase transitions observed. At lower humidity levels, reduced diffraction intensities indicated loss of crystallinity, which was full

SUBMITTER: Kontarinis A 

PROVIDER: S-EPMC12810493 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature