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Iterative screen optimization maximizes the efficiency of macromolecular crystallization
Author(s) -
Jones Harrison G.,
Wrapp Daniel,
Gilman Morgan S. A.,
Battles Michael B.,
Wang Nianshuang,
Sacerdote Sofia,
Chuang Gwo-Yu,
Kwong Peter D.,
McLellan Jason S.
Publication year - 2019
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18017338
Subject(s) - crystallization , computer science , throughput , macromolecule , chemistry , engineering , chemical engineering , biochemistry , telecommunications , wireless
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.