Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 75, Issue -, Pages 123-131Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X18017338
Keywords
automated liquid handling; crystallization screening; macromolecular crystallography; Sweet16
Funding
- Intramural Research Program of the Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
- National Institute of General Medical Sciences [P20GM113132, T32GM008704, 532AI007519]
- 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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