TY - JOUR
TI - In situ detection of a novel lysozyme monoclinic crystal form upon controlled relative humidity variation
AU - Trampari, S.
AU - Valmas, A.
AU - Logotheti, S.
AU - Saslis, S.
AU - Fili, S.
AU - Spiliopoulou, M.
AU - Beckers, D.
AU - Degen, T.
AU - Nénert, G.
AU - Fitch, A.N.
AU - Calamiotou, M.
AU - Karavassili, F.
AU - Margiolaki, I.
JO - Journal of Applied Crystallography
PY - 2018
VL - 51
TODO - 6
SP - 1671-1683
PB - Wiley-Blackwell
SN - 0021-8898, 1600-5767
TODO - 10.1107/S1600576718013936
TODO - 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
TODO - 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.
ER -