Open AccessPurification, crystallization and preliminary X‐ray diffraction analysis of inner membrane complex (IMC) subcompartment protein 1 (ISP1) from Toxoplasma gondii
Author(s) -
Tonkin Michelle L.,
Brown Shan,
Beck Josh R.,
Bradley Peter J.,
Boulanger Martin J.
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911202297x
Subject(s) - toxoplasma gondii , crystallization , chemistry , materials science , crystallography , biology , immunology , antibody , organic chemistry
The protozoan parasites of the Apicomplexa phylum are devastating global pathogens. Their success is largely due to phylum‐specific proteins found in specialized organelles and cellular structures. The inner membrane complex (IMC) is a unique apicomplexan structure that is essential for motility, invasion and replication. The IMC subcompartment proteins (ISP) have recently been identified in Toxoplasma gondii and shown to be critical for replication, although their specific mechanisms are unknown. Structural characterization of Tg ISP1 was pursued in order to identify the fold adopted by the ISPs and to generate detailed insight into how this family of proteins functions during replication. An N‐terminally truncated form of Tg ISP1 was purified from Escherichia coli , crystallized and subjected to X‐ray diffraction analysis. Two crystal forms of Tg ISP1 belonging to space groups P 4 1 32 or P 4 3 32 and P 2 1 2 1 2 1 diffracted to 2.05 and 2.1 Å resolution, respectively.