Preliminary X-ray crystallographic analysis of the complex between the DNAase domain of colicin E9 and its cognate immunity protein

Kühlmann, Ulrike C., Kleanthous, Colin, James, Richard, Moore, Geoffrey R. and Hemmings, Andrew M. (1999) Preliminary X-ray crystallographic analysis of the complex between the DNAase domain of colicin E9 and its cognate immunity protein. Acta Crystallographica Section D: Biological Crystallography, 55 (1). pp. 256-259. ISSN 0907-4449

Full text not available from this repository.

Abstract

We have crystallized and performed preliminary X-ray characterization of the complex between the DNAase domain of the E9 colicin and its cognate immunity protein Im9. The dissociation constant for this complex, K(d) = 1 x 10-16 M, reveals it to be one of the highest affinity protein-protein interactions known. Single crystals of the 1:1 complex were grown from microseeding experiments using PEG 4K as precipitant. The space group is P212121 with one molecule of complex in the asymmetric unit, and crystals contain approximately 43% solvent. These crystals are inherently non-isomorphous and so selenomethionine-derivatized protein has been prepared and crystals grown for MAD phasing experiments.

Item Type:	Article
Uncontrolled Keywords:	structural biology ,/dk/atira/pure/subjectarea/asjc/1300/1315
Faculty \ School:	Faculty of Science > School of Biological Sciences Faculty of Science > School of Chemical Sciences and Pharmacy (former - to 2009)
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	13 Feb 2025 17:30
Last Modified:	16 Feb 2025 06:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/98472
DOI:	10.1107/S0108444998002590

Actions (login required)

View Item