Τίτλος:
In situ detection of a novel lysozyme monoclinic crystal form upon controlled relative humidity variation
Γλώσσες Τεκμηρίου:
Αγγλικά
Περίληψη:
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.
Συγγραφείς:
Trampari, S.
Valmas, A.
Logotheti, S.
Saslis, S.
Fili, S.
Spiliopoulou, M.
Beckers, D.
Degen, T.
Nénert, G.
Fitch, A.N.
Calamiotou, M.
Karavassili, F.
Margiolaki, I.
Περιοδικό:
Journal of Applied Crystallography
Λέξεις-κλειδιά:
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
DOI:
10.1107/S1600576718013936
