ArticleActa crystallographica. Section F, Structural biology communications2019
Iterative screen optimization maximizes the efficiency of macromolecular crystallization.
Article in Acta crystallographica. Section F, Structural biology communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Conformational Diversity-Driven Crystallization of Daptomycin: A Multi-Scale Approach with Experimental Validation.Pharmaceutics · 2026Article
- The FUSION protein crystallization screen.Journal of applied crystallography · 2022Article
- Structural basis for HCMV Pentamer recognition by neuropilin 2 and neutralizing antibodies.Science advances · 2022Article
- High-throughput screening for discovery of benchtop separations systems for selected rare earth elements.Communications chemistry · 2020Article
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Abstract
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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