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A Peltier‐cooled microscope stage for protein crystal post‐crystallization treatment
Author(s) -
Dietl Andreas,
Kieser Christian,
Barends Thomas R. M.
Publication year - 2017
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/s1600576717008755
Subject(s) - mosaicity , protein crystallization , crystallization , microscope , cryoprotectant , crystal (programming language) , materials science , thermoelectric cooling , crystallography , stage (stratigraphy) , diffraction , chemistry , x ray crystallography , optics , thermoelectric effect , thermodynamics , biology , organic chemistry , physics , cryopreservation , embryo , paleontology , computer science , programming language , microbiology and biotechnology
Crystals of the multi‐enzyme complex hydrazine synthase showed severe diffuse scattering and high mosaicity. Improved diffraction quality was achieved by soaking the crystals in highly concentrated betaine solutions at reduced temperatures. To enable this, a Peltier‐cooled microscope stage was developed for the slow cooling of protein crystals immersed in cryoprotectants or other soaking solutions. Both the construction of the stage and its successful application to hydrazine synthase crystals are described.