BIROn - Birkbeck Institutional Research Online

    Crystallization and preliminary X-ray analysis of the uracil-DNA glycosylase DNA repair enzyme from herpes simplex virus type 1

    Savva, Renos and Pearl, L.H. (1993) Crystallization and preliminary X-ray analysis of the uracil-DNA glycosylase DNA repair enzyme from herpes simplex virus type 1. Journal of Molecular Biology 234 (3), pp. 910-912. ISSN 0022-2836.

    Full text not available from this repository.

    Abstract

    A 28·5 kDa catalytic fragment of the uracil-DNA glycosylase DNA repair enzyme from Herpes simplex virus type 1 (HSV-1) has been crystallized using protein from a highly expressing Escherichia coli clone of the Herpes simplex virus type 1 UL2 gene. The protein crystallizes at 12 mg/ml from 11% (w/v) polyethylene glycol 8000 at pH values in the range 6·8 to 7·9, in the presence of (NH4)2SO4. Long trigonal rods (0·08 mm × 0·08 mm × >0·5 mm) diffract beyond 3·0 Å using a laboratory source. The enzyme crystallizes in P31 (or P 32) a = 65·3 Å, c = 49·0 Å with a single molecule in the asymmetric unit and an estimated solvent content of 41% by volume.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Law
    Research Centre: Innovation Management Research, Birkbeck Centre for
    Depositing User: Sarah Hall
    Date Deposited: 14 May 2019 15:34
    Last Modified: 15 Oct 2019 09:03
    URI: http://eprints.bbk.ac.uk/id/eprint/27535

    Statistics

    Downloads
    Activity Overview
    0Downloads
    99Hits

    Additional statistics are available via IRStats2.

    Archive Staff Only (login required)

    Edit/View Item Edit/View Item