ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012
Overproduction, purification and crystallization of PfTic22, a component of the import apparatus from the apicoplast of Plasmodium falciparum.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Cryo-electron tomography reveals four-membrane architecture of the Plasmodium apicoplast.Malaria journal · 2013Article
- Tic22 is an essential chaperone required for protein import into the apicoplast.The Journal of biological chemistry · 2012Article
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Authors and funding
2 authors.
Funding
Abstract
Tic22 is a component of the protein-import apparatus of the chloroplasts of plants and algae and the apicoplasts of the Apicomplexa, a large group of organisms that includes the parasites that cause malaria. Tic22 is important for protein import into these organelles and for organelle biogenesis. It lies between the two membranes of chloroplasts, making interactions with components of both the TIC and TOC complexes. In the apicoplast, it is predicted to be located between the inner two membranes and to play a similar role in import. Although Tic22 is ubiquitous, its function is as yet uncertain. Tic22 from Plasmodium falciparum was therefore overproduced, purified and crystallized. A data set extending to 2.15 Å resolution has been collected from a crystal containing selenomethionine-labelled protein and structure determination is under way.
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