Open AccessHigh‐pressure protein crystallography of hen egg‐white lysozyme
Author(s) -
Yamada Hiroyuki,
Nagae Takayuki,
Watanabe Nobuhisa
Publication year - 2015
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s1399004715000292
Subject(s) - lysozyme , tetragonal crystal system , crystallography , crystal structure , chemistry , crystal (programming language) , internal pressure , molecule , x ray crystallography , protein crystallization , volume (thermodynamics) , egg white , materials science , diffraction , crystallization , thermodynamics , organic chemistry , biochemistry , physics , computer science , optics , composite material , programming language
Crystal structures of hen egg‐white lysozyme (HEWL) determined under pressures ranging from ambient pressure to 950 MPa are presented. From 0.1 to 710 MPa, the molecular and internal cavity volumes are monotonically compressed. However, from 710 to 890 MPa the internal cavity volume remains almost constant. Moreover, as the pressure increases to 950 MPa, the tetragonal crystal of HEWL undergoes a phase transition from P 4 3 2 1 2 to P 4 3 . Under high pressure, the crystal structure of the enzyme undergoes several local and global changes accompanied by changes in hydration structure. For example, water molecules penetrate into an internal cavity neighbouring the active site and induce an alternate conformation of one of the catalytic residues, Glu35. These phenomena have not been detected by conventional X‐ray crystal structure analysis and might play an important role in the catalytic activity of HEWL.