4.0 Article

Iterative screen optimization maximizes the efficiency of macromolecular crystallization

Publisher

INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X18017338

Keywords

automated liquid handling; crystallization screening; macromolecular crystallography; Sweet16

Funding

  1. Intramural Research Program of the Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
  2. National Institute of General Medical Sciences [P20GM113132, T32GM008704, 532AI007519]
  3. NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [ZICAI005112] Funding Source: NIH RePORTER

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Advances in X-ray crystallography have streamlined the process of determining high-resolution three-dimensional macromolecular structures. However, a rate-limiting step in this process continues to be the generation of crystals that are of sufficient size and quality for subsequent diffraction experiments. Here, iterative screen optimization (ISO), a highly automated process in which the precipitant concentrations of each condition in a crystallization screen are modified based on the results of a prior crystallization experiment, is described. After designing a novel high-throughput crystallization screen to take full advantage of this method, the value of ISO is demonstrated by using it to successfully crystallize a panel of six diverse proteins. The results suggest that ISO is an effective method to obtain macromolecular crystals, particularly for proteins that crystallize under a narrow range of precipitant concentrations.

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