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Small angle X-ray scattering and transmission electron microscopy study of the Lactobacillus brevis S-layer protein

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, , Citation Pentti Jääskeläinen et al 2010 J. Phys.: Conf. Ser. 247 012017 DOI 10.1088/1742-6596/247/1/012017

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1 Department of Physics, POB 64, 00014 University of Helsinki, Finland

2 Department of Biomedical Engineering and Computational Science, PO Box 2200, FI-02015 Aalto University School of Science and Technology, Finland

3 Haartman Institute, Department of Pathology, PO Box 21, FIN-00014 University of Helsinki, Finland

4 Department of Basic Veterinary Sciences, Division of Microbiology, FIN-00014 University of Helsinki, Finland

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1742-6596/247/1/012017

Abstract

The structure of self-assembly domain containing recombinant truncation mutants of Lactobacillus brevis surface layer protein SlpA in aqueous solution was studied using small-angle X-ray scattering and transmission electron microscopy. The proteins were found out to interact with each other forming stable globular oligomers of about 10 monomers. The maximum diameter of the oligomers varied between 75 Å and 435 Å.

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10.1088/1742-6596/247/1/012017