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Updated: Sep 27, 2026
High-Throughput Screening to Obtain Crystal Hits for Protein Crystallography
Published on: March 10, 2023
Using rational screening and electron microscopy to optimize the crystallization of succinate:ubiquinone
Rob Horsefield1, Victoria Yankovskaya, Susanna Törnroth
1Department of Biological Sciences, Imperial College, London SW7 2AZ, England.
Abstract:
The membrane-bound respiratory complex II, succinate:ubiquinone oxidoreductase (SQR) from Escherichia coli, has been anaerobically expressed, then purified and crystallized. The initial crystals obtained were small and diffracted poorly. In order to facilitate structure determination, rational screening and sample-quality analysis using electron microscopy was implemented. The crystals of SQR from E. coli belong to the trigonal space group R32, with unit-cell parameters a = b = 138.7, c = 521.9 A, and diffract to 2.6 A resolution. The optimization strategy used for obtaining well diffracting SQR crystals is applicable to a wide range of membrane proteins.
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