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Updated: Aug 15, 2026

Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes
Published on: November 1, 2012
Crystal engineering: a case study using the 24 kDa fragment of the DNA gyrase B subunit from Escherichia coli
A D'Arcy1, M Stihle, D Kostrewa
1F. Hoffmann-La Roche Ltd Pharmaceutical Research, Chemical Technologies, CH-4070, Basel, Switzerland.
Abstract:
Site-directed mutagenesis was used to determine the efficacy of changing surface residues to improve crystal quality. Nine mutants of the 24 kDa fragment of the Escherichia coli DNA gyrase B subunit were produced, changing residues on the protein's surface. The mutations changed either the charge or the polarity of the wild-type amino acid. It was found that single amino-acid changes on the surface could have a dramatic effect on the crystallization properties of the protein and generally resulted in an improvement in the number of crystal-screen hits as well as an improvement in crystal quality. It is concluded that crystal engineering is a valuable tool for protein crystallography.
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