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Crystallization and preliminary crystallographic analysis of a surface antigen glycoprotein, SAG19, from Eimeria tenella
Journal
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Date Issued
2013
Author(s)
Ramly N.Z.
Rouzheinikov S.N.
Sedelnikova S.E.
Baker P.J.
Chow Y.-P.
Wan K.-L.
Nathan S.
Rice D.W.
DOI
10.1107/S1744309113029734
Abstract
Coccidiosis in chickens is caused by the apicomplexan parasite Eimeria tenella and is thought to involve a role for a superfamily of more than 20 cysteine-rich surface antigen glycoproteins (SAGs) in host-parasite interactions. A representative member of the family, SAG19, has been overexpressed in Escherichia coli, purified and crystallized by the hanging-drop method of vapour diffusion using ammonium sulfate as the precipitant. Crystals of SAG19 diffracted to beyond 1.50� resolution and belonged to space group I4, with unit-cell parameters a = b = 108.2, c = 37.5�. Calculation of possible values of V M suggests that there is a single molecule in the asymmetric unit. � 2013 International Union of Crystallography.
Subjects