%0 Journal Article
%A Kallio, Juha
%A Kursula, Inari
%T Recombinant Production, Purification and Crystallization of the Toxoplasma Gondii Coronin WD40 Domain
%J Acta crystallographica / F
%V 70
%@ 1744-3091
%C Oxford [u.a.]
%I Blackwell
%M PUBDB-2015-01354
%P 517-521
%D 2014
%Z (c) International Union of Crystallography. Post referee full text in progress.
%X Toxoplasma gondii is one of the most widely spread parasitic organisms in the world. Together with other apicomplexan parasites, it utilizes a special actin-myosin motor for its cellular movement, called gliding motility. This actin-based process is regulated by a small set of actin-binding proteins, which in Apicomplexa comprises only 10-15 proteins, compared with >150 in higher eukaryotes. Coronin is a highly conserved regulator of the actin cytoskeleton, but its functions, especially in parasites, have remained enigmatic. Coronins consist of an N-terminal actin-binding β-propeller WD40 domain, followed by a conserved region, and a C-terminal coiled-coil domain implicated in oligomerization. Here, the WD40 domain and the conserved region of coronin from <i>T</i>. <i>gondii</i> were produced recombinantly and crystallized. A single-wavelength diffraction data set was collected to a resolution of 1.65 Å. The crystal belonged to the orthorhombic space group C222<sub>1</sub>, with unit-cell parameters <i>a</i> = 55.13, <i>b</i> = 82.51, <i>c</i> = 156.98 Å.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000333757800026
%$ pmid:24699753
%R 10.1107/S2053230X14005196
%U https://bib-pubdb1.desy.de/record/207456