4.3 Article

The FUSION protein crystallization screen

Journal

JOURNAL OF APPLIED CRYSTALLOGRAPHY
Volume 55, Issue -, Pages 310-319

Publisher

INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1600576722001765

Keywords

X-ray crystallography; macromolecular crystallization; crystallization screens; protein crystals

Funding

  1. Medical Research Council, as part of United Kingdom Research and Innovation

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The FUSION protein crystallization screen formulation is an innovative approach that integrates the most efficient components from three existing screens to produce high-quality crystals. It combines 96 unique combinations of crystallization additives, many of which are frequently found in crystal structures of proteins. The efficiency of FUSION is demonstrated by obtaining high yields of diffraction-quality crystals for seven different test proteins, including the discovery of two crystal forms not currently in the Protein Data Bank.
The success and speed of atomic structure determination of biological macromolecules by X-ray crystallography depends critically on the availability of diffraction-quality crystals. However, the process of screening crystallization conditions often consumes large amounts of sample and time. An innovative protein crystallization screen formulation called FUSION has been developed to help with the production of useful crystals. The concept behind the formulation of FUSION was to combine the most efficient components from the three MORPHEUS screens into a single screen using a systematic approach. The resulting formulation integrates 96 unique combinations of crystallization additives. Most of these additives are small molecules and ions frequently found in crystal structures of the Protein Data Bank (PDB), where they bind proteins and complexes. The efficiency of FUSION is demonstrated by obtaining high yields of diffraction-quality crystals for seven different test proteins. In the process, two crystal forms not currently in the PDB for the proteins alpha-amylase and avidin were discovered.

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