Role of Ca2+ in folding the tandem β-sandwich extender domains of a bacterial ice-binding adhesin
Version of Record online: 11 OCT 2013
© 2013 FEBS
The FEBS Journal
Volume 280, Issue 22, pages 5919–5932, November 2013
How to Cite
Guo, S., Garnham, C. P., Karunan Partha, S., Campbell, R. L., Allingham, J. S. and Davies, P. L. (2013), Role of Ca2+ in folding the tandem β-sandwich extender domains of a bacterial ice-binding adhesin. The FEBS Journal, 280: 5919–5932. doi: 10.1111/febs.12518
- Issue online: 24 OCT 2013
- Version of Record online: 11 OCT 2013
- Accepted manuscript online: 11 SEP 2013 08:04AM EST
- Manuscript Accepted: 2 SEP 2013
- Manuscript Revised: 24 AUG 2013
- Manuscript Received: 14 MAY 2013
- R. Samuel McLaughlin fellowship
Fig. S1. Intramolecular Ca2+ ions that are weakly bound to the RII monomer (P1).
Fig. S2. Water molecules that coordinate Ca2+ 2 and 3 are stabilized by neighboring protein ligands and water molecules.
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