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The FUSION protein crystallization screen

DOI: 10.1107/S1600576722001765 DOI Help

Authors: Fabrice Gorrec (MRC Laboratory of Molecular Biology) , Dom Bellini (MRC Laboratory of Molecular Biology)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Applied Crystallography , VOL 55 , PAGES 310 - 319

State: Published (Approved)
Published: April 2022
Diamond Proposal Number(s): 21426

Open Access Open Access

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.

Journal Keywords: X-ray crystallography; macromolecular crystallization; crystallization screens; protein crystals

Subject Areas: Biology and Bio-materials


Instruments: I04-Macromolecular Crystallography

Added On: 16/05/2022 13:07

Documents:
ei5076.pdf

Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)