ArticleJournal of applied crystallography2022
The FUSION protein crystallization screen.
Article in Journal of applied crystallography, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- Crystal structures of the sweet-tasting protein honey truffle active component from Mattirolomyces terfezioides.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Structure of the Arabidopsis receptor kinase SRF6 ectodomain determined from crystals obtained using the LRR crystallization screen.Acta crystallographica. Section D, Structural biology · 2026Article
- Crystal structure of HERV-K envelope glycoprotein surface subunit.Journal of virology · 2026Article
- Structural and functional insights into TBC1D17 highlight the importance of the previously uncharacterized Rab-binding domain.Protein science : a publication of the Protein Society · 2026Article
- Crystal structure of a tRNA acceptor-stem mimic at 1.94 Å resolution.Acta crystallographica. Section F, Structural biology communications · 2026Article
- A generic cross-seeding approach to protein crystallization.Journal of applied crystallography · 2025Article
- High-throughput structure determination of an intrinsically disordered protein using cell-free protein crystallization.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
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2 authors at 1 institution in 1 country.
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Abstract
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 α-amylase and avidin were discovered.
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