1. Crystallization and preliminary crystallographic analysis of a surface antigen glycoprotein, SAG19, from Eimeria tenella.
- Author
-
Ramly NZ, Rouzheinikov SN, Sedelnikova SE, Baker PJ, Chow YP, Wan KL, Nathan S, and Rice DW
- Subjects
- Amino Acid Sequence, Ammonium Sulfate chemistry, Antigens, Surface genetics, Antigens, Surface metabolism, Crystallization, Crystallography, X-Ray, Eimeria tenella genetics, Eimeria tenella metabolism, Escherichia coli genetics, Escherichia coli metabolism, Gene Expression, Molecular Sequence Data, Protozoan Proteins genetics, Protozoan Proteins metabolism, Recombinant Proteins chemistry, Recombinant Proteins genetics, Recombinant Proteins metabolism, Antigens, Surface chemistry, Eimeria tenella chemistry, Protozoan Proteins chemistry
- 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 Å resolution and belonged to space group I4, with unit-cell parameters a = b = 108.2, c = 37.5 Å. Calculation of possible values of VM suggests that there is a single molecule in the asymmetric unit.
- Published
- 2013
- Full Text
- View/download PDF