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Expression, purification and crystallization of the C-terminal LRR domain of Streptococcus pyogenes protein 0843.


ABSTRACT: Streptococcus pyogenes protein 0843 (Spy0843) is a recently identified protein with a potential adhesin function. Sequence analysis has shown that Spy0843 contains two leucine-rich repeat (LRR) domains that mediate interactions with the gp340 receptor. Here, the C-terminal LRR domain was overexpressed in Escherichia coli, purified and crystallized in the presence of 1.7-1.8?M ammonium sulfate pH 7.4 as precipitant. Data were collected from a single crystal to 1.59?Å resolution at 100?K at a synchrotron-radiation source. The crystal was found to belong to space group I41, with unit-cell parameters a = b = 121.4, c = 51.5?Å and one molecule in the asymmetric unit. Elucidation of the crystal structure will provide insights into the interactions of Spy0843 with the gp340 receptor and a better understanding of the role of Spy0843 in streptococcal infections.

SUBMITTER: Haikarainen T 

PROVIDER: S-EPMC3660901 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature

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Expression, purification and crystallization of the C-terminal LRR domain of Streptococcus pyogenes protein 0843.

Haikarainen Teemu T   Loimaranta Vuokko V   Prieto-Lopez Carlos C   Battula Pradeep P   Finne Jukka J   Papageorgiou Anastassios C AC  

Acta crystallographica. Section F, Structural biology and crystallization communications 20130430 Pt 5


Streptococcus pyogenes protein 0843 (Spy0843) is a recently identified protein with a potential adhesin function. Sequence analysis has shown that Spy0843 contains two leucine-rich repeat (LRR) domains that mediate interactions with the gp340 receptor. Here, the C-terminal LRR domain was overexpressed in Escherichia coli, purified and crystallized in the presence of 1.7-1.8 M ammonium sulfate pH 7.4 as precipitant. Data were collected from a single crystal to 1.59 Å resolution at 100 K at a sync  ...[more]

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