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Frontiers Media, Frontiers in Microbiology, (6), 2015

DOI: 10.3389/fmicb.2015.00414

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Purification and characterization of DR_2577 (SlpA) a major S-layer protein from Deinococcus radiodurans

Journal article published in 2015 by Domenica Farci, Mw Bowler, Francesca Esposito, Sean McSweeney, Enzo Tramontano ORCID, Dario Piano
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

The protein DR_2577 is a major Surface layer component of the radio-resistant bacterium Deinococcus radiodurans. In the present study DR_2577 has been purified and its oligomeric profile characterized by means of size exclusion chromatography and gel electrophoresis. DR_2577 was found to be organized into three hierarchical orders characterized by monomers, stable dimers formed by the occurrence of disulphide bonds, and hexamers resulting from a combination of dimers. The structural implications of these findings are discussed providing new elements for a more integrated model of this S-layer.