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On the preparation and X‐ray data collection of isomorphous xenon derivatives
Author(s) -
Schiltz M.,
Prangé T.,
Fourme R.
Publication year - 1994
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889894005923
Subject(s) - xenon , absorption (acoustics) , chemistry , protein crystallization , crystal (programming language) , x ray , crystallography , diffraction , hydrate , materials science , analytical chemistry (journal) , crystallization , optics , chromatography , physics , organic chemistry , computer science , composite material , programming language
A simple method for the preparation of isomorphous xenon derivatives is presented. A device has been designed that allows diffraction studies on protein crystals under xenon gas pressures up to 50 × 10 5 Pa. Crystal mounting and X‐ray data collection do not significantly differ from standard techniques. Tests carried out on crystals of the protein porcine pancreatic elastase reveal a single xenon binding site with high occupancy at a pressure of 8 × 10 5 Pa. Xenon binding to several other crystallized proteins has also been investigated and results indicate that the method is generally applicable. Time‐resolved studies show that, at 297 K, xenon binding is essentially completed within a few minutes. At pressures above 10 6 Pa, successful data collection is hampered by X‐ray absorption and by the formation of xenon hydrate. Absorption can be reduced by using short‐wavelength radiation and by mounting crystals in small capillaries. To circumvent xenon hydrate formation, higher working temperatures and the use of cryoprotective mother liquors are advocated.