Crystallization and preliminary crystallographic analysis of a surface antigen glycoprotein, SAG19, from Eimeria tenella

• Main Authors: Sergey N., Rouzheinikov,, Svetlana E., Sedelnikova,, Patrick J., Baker,, David W., Rice,, Nur Zazarina, Ramly,, Yock-Ping, Chow,, Kiew-Lian, Wan,, Sheila, Nathan,
• Format: Article
• Language: English
• Published: International Union of Crystallography 2015
• Subjects: Toxoplasma-Gondii; Srs Superfamily; Proteins; Coccidiosis

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 angstrom resolution and belonged to space group I4, with unit-cell parameters a = b = 108.2, c = 37.5 angstrom. Calculation of possible values of V-M suggests that there is a single molecule in the asymmetric unit.