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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Veröffentlicht in:	Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2012-12, Vol.68 (12), p.1511-1514
Hauptverfasser:	Đordić, Anđela, Egelseer, Eva M., Tesarz, Manfred, Sleytr, Uwe B., Keller, Walter, Pavkov-Keller, Tea
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Proteins - chemistry Bacterial Proteins - metabolism Cell Wall - metabolism Construction Crystal structure Crystallization Crystallization Communications Crystallography, X-Ray Crystals Diffraction Geobacillus stearothermophilus Geobacillus stearothermophilus - metabolism Membrane Glycoproteins - chemistry Membrane Glycoproteins - metabolism Protein Structure, Tertiary Proteins Recombinant S-layer Self assembly
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Zusammenfassung:	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.
ISSN:	1744-3091 1744-3091 2053-230X
DOI:	10.1107/S1744309112042650