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Journal Article

A Peltier-cooled microscope stage for protein crystal post-crystallization treatment

MPS-Authors
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Dietl,  Andreas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Kieser,  Christian
Electronics Laboratory, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons92083

Barends,  Thomas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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https://onlinelibrary.wiley.com/doi/pdf/10.1107/S1600576717008755
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https://doi.org/10.1107/S1600576717008755
(Any fulltext)

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Citation

Dietl, A., Kieser, C., & Barends, T. (2017). A Peltier-cooled microscope stage for protein crystal post-crystallization treatment. Journal of Applied Crystallography, 50(4), 1208-1211. doi:10.1107/S1600576717008755.


Cite as: https://hdl.handle.net/21.11116/0000-0001-4249-3
Abstract
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.