Crystallization and preliminary crystallographic analysis of a surface antigen glycoprotein, SAG19, from Eimeria tenella. Issue 12 (1st December 2013)

• Record Type: Journal Article
• Authors: Ramly, Nur Zazarina; Rouzheinikov, Sergey N.; Sedelnikova, Svetlana E.; Baker, Patrick J.; Chow, Yock‐Ping; Wan, Kiew‐Lian; Nathan, Sheila; Rice, David W.
• Is Part Of: Acta crystallographica. Volume 69:Issue 12(2013:Dec.)
• Page Start: 1380
• Page End: 1383
• Publication Date: 2013-12-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113029734
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Coccidiosis in chickens is caused by the apicomplexan parasite <italic>Eimeria tenella</italic> 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 <italic>Escherichia coli</italic>, 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 <italic>I</italic>4, with unit‐cell parameters <italic>a</italic> = <italic>b</italic> = 108.2, <italic>c</italic> = 37.5 Å. Calculation of possible values of <italic>V</italic>_M suggests that there is a single molecule in the asymmetric unit.</p> </abstract>