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Updated: Jan 13, 2026

Electron Cryotomography of Bacterial Cells
Published on: May 6, 2010
Comparative Structural Analysis of Escherichia Coli Cyay at Room and Cryogenic Temperatures Using Macromolecular and
Alaleh Shafiei1, Nilufer Baldir1, Jongbum Na2
1Department of Molecular Biology and Genetics, Koc University, 34450, Istanbul, Turkey.
None:
Frataxin is a 23 kDa mitochondrial iron-binding protein involved in the biogenesis of iron-sulfur (Fe-S) clusters. Deficiency in frataxin is associated with Friedreich's ataxia, a progressive neurodegenerative disorder. CyaY, the bacterial ortholog of eukaryotic frataxin, is believed to function as an iron donor in Fe-S cluster assembly, making it a key target for structural and functional studies. In this work, a comprehensive structural analysis of the Escherichia coli CyaY protein is presented, comparing its structure at room temperature and cryogenic conditions. Notably, the first room-temperature structures are obtained using the Turkish Light Source "Turkish DeLight" X-ray diffractometer and serial synchrotron X-ray crystallography, marking a significant step forward in understanding CyaY under near-physiological conditions.
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