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

Dominique Monferrer, Tewes Tralau, Michael A. Kertesz, Santosh Panjikar, Isabel Usón

    Research output: Contribution to journalArticlepeer-review

    Abstract

    The 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.
    Original languageEnglish
    Pages (from-to)764-769
    Number of pages5
    JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
    Volume64
    Issue number8
    DOIs
    Publication statusPublished - 2008

    Keywords

    • Full-length LysR-type regulator
    • Microbatch crystallization
    • MIRAS phasing

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