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

MPG-Autoren
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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;

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

Externe Ressourcen

https://onlinelibrary.wiley.com/doi/pdf/10.1107/S1600576717008755
(beliebiger Volltext)

https://doi.org/10.1107/S1600576717008755
(beliebiger Volltext)

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Zitation

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.


Zitierlink: https://hdl.handle.net/21.11116/0000-0001-4249-3
Zusammenfassung
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.