The FUSION protein crystallization screen.
Authors
Gorrec, Fabrice
Bellini, Dom
Publication Date
2022-04-01Journal Title
J Appl Crystallogr
ISSN
0021-8898
Publisher
International Union of Crystallography (IUCr)
Language
en
Type
Article
This Version
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Gorrec, F., & Bellini, D. (2022). The FUSION protein crystallization screen.. J Appl Crystallogr https://doi.org/10.1107/S1600576722001765
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.
Keywords
X-ray crystallography, crystallization screens, macromolecular crystallization, protein crystals
Identifiers
jcr2ei5076, ei5076
External DOI: https://doi.org/10.1107/S1600576722001765
This record's URL: https://www.repository.cam.ac.uk/handle/1810/334903
Rights
Licence:
http://creativecommons.org/licenses/by/4.0/
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