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High crystallizability under air-exclusion conditions of the full-length LysR-type transcriptional regulator TsaR from Comamonas testosteroni T-2 and data-set analysis for a MIRAS structure-solution approach

AuthorsMonferrer, Dominique; Tralau, Tewes; Kertesz, Michael; Panjikar, Santosh; Usón, Isabel
KeywordsMicrobatch crystallization
Full-length LysR-type regulator
MIRAS phasing
Issue Date1-Sep-2008
PublisherInternational Union of Crystallography
CitationActa Crystallographica Section F: Structural Biology and Crystallization Communications 64(8): 764-769 (2008)
AbstractThe full-length LysR-type transcriptional regulator TsaR from Comamonas testosteroni T-2 was heterologously overexpressed in Escherichia coli, purified and stabilized under conditions that favoured its rapid crystallization using the microbatch-under-oil technique. The purified protein was highly crystallizable and two different crystal forms were readily obtained. However, only monoclinic crystals gave diffraction beyond 2 Å and there was a slight variation in unit-cell parameters between crystals. The only other LysR-type regulator for which a full-length crystal form is available is CbnR, but no solution could be obtained when this was used as a model in molecular replacement. Mercury and xenon derivatives were therefore produced in order to phase the structure using a MIRAS approach. © International Union of Crystallography 2008.
Publisher version (URL)http://dx.doi.org/10.1107/S1744309108019738
Identifiersdoi: 10.1107/S1744309108019738
issn: 1744-3091
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