Published August 5, 1993
| public
Journal Article
Crystallization and preliminary X-ray analysis of the DNA binding domain of the Hin recombinase with its DNA binding site
Abstract
The Hin recombinase catalyzes site-specific inversion of DNA. Chemical and genetic studies on Hin binding to the recombination sites indicates that both major and minor DNA groove interactions are critical. In order to determine the molecular nature of these interactions, we have crystallized a synthetically derived 52 amino acid peptide consisting of the DNA binding domain of Hin with a 14 base-pair oligonucleotide representing a recombination half-site. This communication presents preliminary diffraction and analysis of these cocrystals and a packing model for the complex within the crystal.
Additional Information
© 1993 Academic Press. Received 26 October 1992; accepted 16 March 1993. We thank Dohn Glitz for advice and help in DNA synthesis, and Steven Finkel for help in DNA synthesis and purification. We also thank Duilio Cascio for assistance in data collection. This work was carried out with the support of research grants NIH GM-31299 to R.E.D., GM-38509 to R.C.J. and NSF grant DMB-8516021 to M.S.Additional details
- Eprint ID
- 66931
- DOI
- 10.1006/jmbi.1993.1443
- Resolver ID
- CaltechAUTHORS:20160510-140054373
- GM-31299
- NIH
- GM-38509
- NIH
- DMB-8516021
- NSF
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2016-05-19Created from EPrint's datestamp field
- Updated
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2021-11-11Created from EPrint's last_modified field