ArticleBiomolecules2026
In Situ XRPD Investigation of Relative Humidity-Induced Lattice Responses in Tetragonal Hen Egg-White Lysozyme.
Article in Biomolecules, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Protein crystals are intrinsically hydrated systems, and their structural integrity is strongly influenced by environmental humidity. Understanding the effects of relative humidity (RH) variation on crystal stability is therefore essential for both fundamental research and applied studies. In this work, the structural response of tetragonal hen egg-white lysozyme (HEWL) to controlled RH variation was investigated using in situ X-ray powder diffraction (XRPD). Polycrystalline HEWL samples were subjected to systematic gradual dehydration and rehydration cycles, as well as to non-gradual RH variation protocols. Pawley analysis of the XRPD data enabled monitoring of the evolution of unit cell parameters and unit cell volume as a function of RH. Under all experimental conditions, the tetragonal polymorph (space group
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