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    Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Dec 1;64(Pt 12):1184-7. Epub 2008 Nov 28.

    Purification, crystallization and preliminary X-ray diffraction analysis of the HMG domain of Sox17 in complex with DNA.

    Ng CK, Palasingam P, Venkatachalam R, Baburajendran N, Cheng J, Jauch R, Kolatkar PR.

    Source

    Laboratory for Structural Biochemistry, Genome Institute of Singapore, Genome, 60 Biopolis Street, Singapore 138672, Singapore.

    Abstract

    Sox17 is a member of the SRY-related high-mobility group (HMG) of transcription factors that have been shown to direct endodermal differentiation in early mammalian development. The LAMA1 gene encoding the alpha-chain of laminin-1 has been reported to be directly bound and regulated by Sox17. This paper describes the details of initial crystallization attempts with the HMG domain of mouse Sox17 (mSox17-HMG) with a 16-mer DNA element derived from the LAMA1 enhancer and optimization strategies to obtain a better diffracting crystal. The best diffracting crystal was obtained in a condition containing 0.1 M Tris-HCl pH 7.4, 0.2 M MgCl(2), 30% PEG 3350 using the hanging-drop vapour-diffusion method. A highly redundant in-house data set was collected to 2.75 A resolution with 99% completeness. The presence of the mSox17-HMG-DNA complex within the crystals was confirmed and Matthews analysis indicated the presence of one complex per asymmetric unit.

    PMID:
    19052383
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2593696
    Free PMC Article

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