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

Pentti Jääskeläinen; Peter Engelhardt; Ulla Hynönen; Mika Torkkeli; Airi Palva; Ritva Serimaa

doi:10.1088/1742-6596/247/1/012017

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

Pentti Jääskeläinen^*, Peter Engelhardt, Ulla Hynönen, Mika Torkkeli, Airi Palva, Ritva Serimaa

^*Corresponding author for this work

University of Helsinki

Research output: Contribution to journal › Article › Scientific › peer-review

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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 and 435 .

Original language	English
Article number	012017
Journal	Journal of Physics: Conference Series
Volume	247
DOIs	https://doi.org/10.1088/1742-6596/247/1/012017
Publication status	Published - 2010
MoE publication type	A1 Journal article-refereed

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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 and 435 .",

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AU - Jääskeläinen, Pentti

AU - Engelhardt, Peter

AU - Hynönen, Ulla

AU - Torkkeli, Mika

AU - Palva, Airi

AU - Serimaa, Ritva

PY - 2010

Y1 - 2010

N2 - 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 and 435 .

AB - 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 and 435 .

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U2 - 10.1088/1742-6596/247/1/012017

DO - 10.1088/1742-6596/247/1/012017

M3 - Article

AN - SCOPUS:78651074947

SN - 1742-6588

VL - 247

JO - Journal of Physics: Conference Series

JF - Journal of Physics: Conference Series

M1 - 012017

ER -

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

Abstract

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