@article{3086622,
    title = "In situ detection of a novel lysozyme monoclinic crystal form upon controlled relative humidity variation",
    author = "Trampari, S. and Valmas, A. and Logotheti, S. and Saslis, S. and Fili, S. and Spiliopoulou, M. and Beckers, D. and Degen, T. and Nénert, G. and Fitch, A.N. and Calamiotou, M. and Karavassili, F. and Margiolaki, I.",
    journal = "Journal of Applied Crystallography",
    year = "2018",
    volume = "51",
    number = "6",
    pages = "1671-1683",
    publisher = "Wiley-Blackwell",
    issn = "0021-8898, 1600-5767",
    doi = "10.1107/S1600576718013936",
    keywords = "Diffraction;  Enzymes;  Humidity control;  X ray powder diffraction;  X rays, Drug development;  Hen egg white lysozyme;  Humidity levels;  In-situ detections;  Monoclinic crystals;  Powder diffraction;  Protein crystallization;  Structural modifications, X ray crystallography",
    abstract = "The effect of relative humidity (rH) on protein crystal structures, an area that has attracted high scientific interest during the past decade, is investigated in this study on hen egg-white lysozyme (HEWL) polycrystalline precipitates via in situ laboratory X-ray powder diffraction (XRPD) measurements. For this purpose, HEWL was crystallized at room temperature and pH 4.5, leading to a novel monoclinic HEWL phase which, to our knowledge, has not been reported before. Analysis of XRPD data collected upon rH variation revealed several structural modifications. These observations, on a well-studied molecule like HEWL, underline not only the high impact of humidity levels on biological crystal structures, but also the significance of in-house XRPD as an analytical tool in industrial drug development and its potential to provide information for enhancing manufacturing of pharmaceuticals. © 2018 International Union of Crystallography."
}