Open AccessCrystallization and preliminary crystallographic analysis of a surface antigen glycoprotein, SAG19, from Eimeria tenella
Author(s) -
Ramly Nur Zazarina,
Rouzheinikov Sergey N.,
Sedelnikova Svetlana E.,
Baker Patrick J.,
Chow YockPing,
Wan KiewLian,
Nathan Sheila,
Rice David W.
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113029734
Subject(s) - eimeria , crystallization , ammonium sulfate , glycoprotein , antigen , parasite hosting , crystallography , chemistry , escherichia coli , biology , coccidiosis , biochemistry , microbiology and biotechnology , gene , genetics , chromatography , organic chemistry , world wide web , computer science , medicine , veterinary medicine
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 I 4, with unit‐cell parameters a = b = 108.2, c = 37.5 Å. Calculation of possible values of V M suggests that there is a single molecule in the asymmetric unit.