Crystallization of domains involved in self-assembly of the S-layer protein SbsC

The Gram-positive bacterium Geobacillus stearothermophilus ATCC 12980 is completely covered with a two-dimensional crystalline monolayer composed of the S-layer protein SbsC. In order to complete the structure of the full-length protein, additional soluble constructs containing the crucial domains f...

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Detalles Bibliográficos
Autores principales: Đordić, Anđela, Egelseer, Eva M., Tesarz, Manfred, Sleytr, Uwe B., Keller, Walter, Pavkov-Keller, Tea
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2012
Materias:
Crystallization Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3509976/
https://www.ncbi.nlm.nih.gov/pubmed/23192035
http://dx.doi.org/10.1107/S1744309112042650
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author Đordić, Anđela
Egelseer, Eva M.
Tesarz, Manfred
Sleytr, Uwe B.
Keller, Walter
Pavkov-Keller, Tea
author_facet Đordić, Anđela
Egelseer, Eva M.
Tesarz, Manfred
Sleytr, Uwe B.
Keller, Walter
Pavkov-Keller, Tea
author_sort Đordić, Anđela
collection PubMed
description The Gram-positive bacterium Geobacillus stearothermophilus ATCC 12980 is completely covered with a two-dimensional crystalline monolayer composed of the S-layer protein SbsC. In order to complete the structure of the full-length protein, additional soluble constructs containing the crucial domains for self-assembly have been successfully cloned, expressed and purified. Crystals obtained from three different recombinant constructs yielded diffraction to 3.4, 2.8 and 1.5 Å resolution. Native data have been collected.
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spelling pubmed-35099762012-12-11 Crystallization of domains involved in self-assembly of the S-layer protein SbsC Đordić, Anđela Egelseer, Eva M. Tesarz, Manfred Sleytr, Uwe B. Keller, Walter Pavkov-Keller, Tea Acta Crystallogr Sect F Struct Biol Cryst Commun Crystallization Communications The Gram-positive bacterium Geobacillus stearothermophilus ATCC 12980 is completely covered with a two-dimensional crystalline monolayer composed of the S-layer protein SbsC. In order to complete the structure of the full-length protein, additional soluble constructs containing the crucial domains for self-assembly have been successfully cloned, expressed and purified. Crystals obtained from three different recombinant constructs yielded diffraction to 3.4, 2.8 and 1.5 Å resolution. Native data have been collected. International Union of Crystallography 2012-11-14 /pmc/articles/PMC3509976/ /pubmed/23192035 http://dx.doi.org/10.1107/S1744309112042650 Text en © Đordić et al. 2012 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Crystallization Communications
Đordić, Anđela
Egelseer, Eva M.
Tesarz, Manfred
Sleytr, Uwe B.
Keller, Walter
Pavkov-Keller, Tea
Crystallization of domains involved in self-assembly of the S-layer protein SbsC
title Crystallization of domains involved in self-assembly of the S-layer protein SbsC
title_full Crystallization of domains involved in self-assembly of the S-layer protein SbsC
title_fullStr Crystallization of domains involved in self-assembly of the S-layer protein SbsC
title_full_unstemmed Crystallization of domains involved in self-assembly of the S-layer protein SbsC
title_short Crystallization of domains involved in self-assembly of the S-layer protein SbsC
title_sort crystallization of domains involved in self-assembly of the s-layer protein sbsc
topic Crystallization Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3509976/
https://www.ncbi.nlm.nih.gov/pubmed/23192035
http://dx.doi.org/10.1107/S1744309112042650
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