High-pressure protein crystallography of hen egg-white lysozyme

Journal Article · Wed Apr 01 04:00:00 EDT 2015 · Acta Crystallographica. Section D: Biological Crystallography

DOI:https://doi.org/10.1107/S1399004715000292· OSTI ID:22347698

Yamada, Hiroyuki; Nagae, Takayuki ^[1]; Watanabe, Nobuhisa ^[1]

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1. Nagoya University, Chikusa, Nagoya, Aichi 464-8603 (Japan)

The crystal structure of hen egg-white lysozyme (HEWL) was analyzed under pressures of up to 950 MPa. The high pressure modified the conformation of the molecule and induced a novel phase transition in the tetragonal crystal of HEWL. 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 P4{sub 3}2{sub 1}2 to P4{sub 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.

• OSTI ID: 22347698
• Journal Information: Acta Crystallographica. Section D: Biological Crystallography, Journal Name: Acta Crystallographica. Section D: Biological Crystallography Journal Issue: Pt 4 Vol. 71; ISSN ABCRE6; ISSN 0907-4449
• Country of Publication: Denmark
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTAL STRUCTURE
CRYSTALLOGRAPHY
CRYSTALS
HYDRATION
LYSOZYME
MOLECULES
PRESSURE RANGE MEGA PA 10-100
WATER