Crystallization and preliminary crystallographic analysis of an Ig-domain-encompassing fragment of the giant adhesion protein SiiE from Salmonella enterica

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Abstract

Salmonella infections can be life-threatening. SiiE is a giant adhesion molecule of 5559 amino acids that is encoded in Salmonella pathogenicity island 4 (SPI4) and that promotes the initial contact between the pathogen and polarized epithelial cells in the intestine of the host. Starting from an engineered deletion version of SiiE (mini-SiiE; 97 kDa), limited proteolysis was used to reproducibly generate a 30 kDa fragment that readily crystallized. Mass spectrometry hints that this fragment spans the predicted Ig domains 50-52 of SiiE. Crystals of both native and selenomethionine-labelled protein could be obtained in space group C2 and diffraction data were recorded to a resolution of 1.85 Å. © 2011 International Union of Crystallography. All rights reserved.

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Sturm, K. U., Griessl, M. H., Wagner, C., Deiwick, J., Hensel, M., & Muller, Y. A. (2011). Crystallization and preliminary crystallographic analysis of an Ig-domain-encompassing fragment of the giant adhesion protein SiiE from Salmonella enterica. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 67(11), 1371–1374. https://doi.org/10.1107/S1744309111032039

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