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.
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 Faculties and Schools > Faculty of Science > School of Natural Sciences |
| Depositing User: | Sarah Hall |
| Date Deposited: | 14 May 2019 15:34 |
| Last Modified: | 02 Aug 2023 17:51 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/27535 |
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