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
Descripción
Sumario: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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