Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt 5):425-7. Epub 2008 Apr 30.
Insect-cell expression, crystallization and X-ray data collection of the bradyzoite-specific antigen BSR4 from Toxoplasma gondii
Grujic O, Grigg ME, Boulanger MJ.
Biochemistry and Microbiology, University of Victoria, PO Box 3055 STN CSC, Victoria, BC, V8W 3P6, Canada.
Toxoplasma gondii is an important global pathogen that infects nearly one third of the world's adult population. A family of developmentally expressed structurally related surface-glycoprotein adhesins (SRSs) mediate attachment to and are utilized for entry into host cells. The latent bradyzoite form of T. gondii persists for the life of the host and expresses a distinct family of SRS proteins, of which the bradyzoite-specific antigen BSR4 is a prototypical member. Structural studies of BSR4 were initiated by first recombinantly expressing BSR4 in insect cells, which was followed by crystallization and preliminary X-ray data collection to 1.95 A resolution. Data processing showed that BSR4 crystallized with one molecule in the asymmetric unit of the P4(1)2(1)2 or P4(3)2(1)2 space group, with a solvent content of 60% and a corresponding Matthews coefficient of 2.98 A(3) Da(-1).
Research Support, Non-U.S. Gov't
PMID: 18453717 [PubMed - in process]