Ramly N.Z.Rouzheinikov S.N.Sedelnikova S.E.Baker P.J.Chow Y.-P.Wan K.-L.Nathan S.Rice D.W.2024-05-292024-05-2920131744309110.1107/S17443091130297342-s2.0-84890066210https://www.scopus.com/inward/record.uri?eid=2-s2.0-84890066210&doi=10.1107%2fS1744309113029734&partnerID=40&md5=ac11ac672582fa7d21b4f159b88b60a4https://oarep.usim.edu.my/handle/123456789/953124316835Coccidiosis 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.en-USapicomplexaEimeria tenellaSAG19Crystallization and preliminary crystallographic analysis of a surface antigen glycoprotein, SAG19, from Eimeria tenellaActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.Article138013836912