Role of D535 and H538 in endogenous toxicity of xenocin from Xenorhabdus nematophila
Version of Record online: 10 DEC 2012
© 2012 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved
FEMS Microbiology Letters
Volume 338, Issue 2, pages 147–154, January 2013
How to Cite
Singh, J. (2013), Role of D535 and H538 in endogenous toxicity of xenocin from Xenorhabdus nematophila. FEMS Microbiology Letters, 338: 147–154. doi: 10.1111/1574-6968.12045
- Issue online: 27 DEC 2012
- Version of Record online: 10 DEC 2012
- Accepted manuscript online: 9 NOV 2012 05:05AM EST
- Manuscript Accepted: 29 OCT 2012
- Manuscript Received: 6 OCT 2012
Fig. S1. Multiple sequence alignment of catalytic domain from different bacteriocins.
Fig. S2. Pair wise sequence alignment of catalytic domain from xenocin with E3.
Fig. S3. Pair wise sequence alignment of catalytic domain from xenocin with Barnase.
Fig. S4. Pair wise sequence alignment of catalytic domain from xenocin with RNase.
Fig. S5. Phylogenetic tree of xenocin from X. nematophila, E. coli E3, pancreatic RNase A and Bacillus Barnase.
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