Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 5 (May 2008)

crystallization communications

Acta Cryst. (2008). F64, 425-427 [ doi:10.1107/S1744309108010920 ]

Insect-cell expression, crystallization and X-ray data collection of the bradyzoite-specific antigen BSR4 from Toxoplasma gondii

O. Grujic, M. E. Grigg and M. J. Boulanger

Abstract: 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 Å resolution. Data processing showed that BSR4 crystallized with one molecule in the asymmetric unit of the P4₁2₁2 or P4₃2₁2 space group, with a solvent content of 60% and a corresponding Matthews coefficient of 2.98 Å³ Da^-1.

Keywords: Toxoplasma gondii; BSR4; bradyzoites; baculovirus.