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A general method for hyperquenching protein crystals

  • Published:
Journal of Structural and Functional Genomics

Abstract

During flash cooling of protein crystals in liquid cryogens, cooling rates are determined by sample size, choice of cooling liquid, and by the thickness of the cold gas layer that forms above the liquid. We describe an experimental protocol for ultra-rapid cooling of protein crystals. This protocol requires no complex apparatus, and yields ice-ring-free diffraction without the use of penetrating cryoprotectants.

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Abbreviations

PFPE:

perflouropolyether

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Acknowledgements

We wish to thank Craig Bingman and George Phillips for assistance in evaluating and improving the protocols described here. This work was supported by the National Institutes of Health (NIH) under award GM065981-05A1. Some experiments were performed at the Cornell High Energy Synchrotron Source (CHESS), which is supported by the National Science Foundation under award DMR 0225180, using the Macromolecular Diffraction at CHESS (MacCHESS) facility, which is supported by award RR-01646 from the National Institutes of Health, through its National Center for Research Resources.

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Authors and Affiliations

  1. Physics Department, Cornell University, Ithaca, NY, 14853, USA

    Matthew Warkentin & Robert E. Thorne

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  1. Matthew Warkentin
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  2. Robert E. Thorne
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Correspondence to Robert E. Thorne.

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Warkentin, M., Thorne, R.E. A general method for hyperquenching protein crystals. J Struct Funct Genomics 8, 141–144 (2007). https://doi.org/10.1007/s10969-007-9029-0

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  • DOI: https://doi.org/10.1007/s10969-007-9029-0

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