%0 Journal Article
%A Shafiei, Alaleh
%A Baldir, Nilufer
%A Na, Jongbum
%A Kim, Jin Kyun
%A DeMirci, Hasan
%T Comparative Structural Analysis of Escherichia Coli Cyay at Room and Cryogenic Temperatures Using Macromolecular and Serial Crystallography
%J ChemBioChem
%V 26
%N 20
%@ 1439-4227
%C Weinheim
%I Wiley-VCH
%M PUBDB-2025-05616
%P e202500442
%D 2025
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%R 10.1002/cbic.202500442
%U https://bib-pubdb1.desy.de/record/642767