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Download Hi-Res ImageDownload to MS-PowerPointCite This:Crystal Growth & Design 2020, 20, 2, 984-994
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    Tailored Suits Fit Better: Customized Protein Crystallization Screens
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    • Georg Mlynek
      Georg Mlynek
      Department of Structural and Computational Biology, Max Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria
      More by Georg Mlynek
    • Julius Kostan
      Julius Kostan
      Department of Structural and Computational Biology, Max Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria
      More by Julius Kostan
    • Sarah Leeb
      Sarah Leeb
      Department of Structural and Computational Biology, Max Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria
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    • Kristina Djinović-Carugo*
      Kristina Djinović-Carugo
      Department of Structural and Computational Biology, Max Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria
      Department of Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, Večna pot 113, SI-1000 Ljubljana, Slovenia
      *Email: [email protected]
      More by Kristina Djinović-Carugo
      Orcidhttp://orcid.org/0000-0003-0252-2972
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    Crystal Growth & Design

    Cite this: Cryst. Growth Des. 2020, 20, 2, 984–994
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    https://doi.org/10.1021/acs.cgd.9b01328
    Published December 31, 2019
    Copyright © 2019 American Chemical Society
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    Abstract

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    The major bottleneck in macromolecular crystallography is the production of well-diffracting crystals. To increase the crystallization success, we developed a crystallization strategy customizable for each protein and tested it on selected model and in-house non-yet-crystallized proteins. The underlying concept is to use in crystallization cocktails compounds that increase the thermal stability of the protein. This customized strategy yielded not only twice as many crystal hits as the standard approach but also crystal hits for two additional proteins compared to the benchmark workflow. The inherently simple design and the modular and flexible nature of the platform makes it easy to modify, further develop, and optimize individual steps. The information gained can also be used to increase the monodispersity and stability of proteins, improving in this way their amenability for biochemical studies and eventually derive a possible function of not yet annotated proteins.

    Copyright © 2019 American Chemical Society

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    Supporting Information

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    The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acs.cgd.9b01328.

    • Examples of representative SEC profiles; Crystals of selected proteins; Overview of results of the crystallization trials; List of proteins and their properties, list of buffers, their pH, and concentration used in the DSF-buffer/pH screen, and list of additives used in the DSF-additive screen; Effect/importance of crystallization compounds on crystallization of individual proteins; Number of hits and crystallization rate of “recalcitrant to crystallize” (PDF)

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    Cited By

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    This article is cited by 2 publications.

    1. Marton Palatinszky, Craig W. Herbold, Christopher J. Sedlacek, Dominic Pühringer, Katharina Kitzinger, Andrew T. Giguere, Kenneth Wasmund, Per H. Nielsen, Morten K. D. Dueholm, Nico Jehmlich, Richard Gruseck, Anton Legin, Julius Kostan, Nesrete Krasnici, Claudia Schreiner, Johanna Palmetzhofer, Thilo Hofmann, Michael Zumstein, Kristina Djinović-Carugo, Holger Daims, Michael Wagner. Growth of complete ammonia oxidizers on guanidine. Nature 2024, 633 (8030) , 646-653. https://doi.org/10.1038/s41586-024-07832-z
    2. Julius Kostan, Miha Pavšič, Vid Puž, Thomas C. Schwarz, Friedel Drepper, Sibylle Molt, Melissa Ann Graewert, Claudia Schreiner, Sara Sajko, Peter F. M. van der Ven, Adekunle Onipe, Dmitri I. Svergun, Bettina Warscheid, Robert Konrat, Dieter O. Fürst, Brigita Lenarčič, Kristina Djinović-Carugo, . Molecular basis of F-actin regulation and sarcomere assembly via myotilin. PLOS Biology 2021, 19 (4) , e3001148. https://doi.org/10.1371/journal.pbio.3001148
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    Crystal Growth & Design

    Cite this: Cryst. Growth Des. 2020, 20, 2, 984–994
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acs.cgd.9b01328
    Published December 31, 2019
    Copyright © 2019 American Chemical Society
    Request reuse permissions

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