A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Expression, purification and crystallization of the C-terminal LRR domain of Streptococcus pyogenes protein 0843
Tekijät: Haikarainen T, Loimaranta V, Prieto-Lopez C, Battula P, Finne J, Papageorgiou AC
Kustantaja: WILEY-BLACKWELL
Julkaisuvuosi: 2013
Journal: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Tietokannassa oleva lehden nimi: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS
Lehden akronyymi: ACTA CRYSTALLOGR F
Numero sarjassa: 5
Vuosikerta: 69
Numero: 5
Aloitussivu: 559
Lopetussivu: 561
Sivujen määrä: 3
ISSN: 1744-3091
DOI: https://doi.org/10.1107/S1744309113009664
Verkko-osoite: http://scripts.iucr.org/cgi-bin/paper?S1744309113009664
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 angstrom resolution at 100 K at a synchrotron-radiation source. The crystal was found to belong to space group I4(1), with unit-cell parameters a = b = 121.4, c = 51.5 angstrom 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.
