PMID:10930845
| Citation |
Lee, MG, Cho, SJ, Yang, JK, Song, HK and Suh, SW (2000) Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli CyaY, a structural homologue of human frataxin. Acta Crystallogr. D Biol. Crystallogr. 56:920-1 |
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| Abstract |
CyaY is a 106-residue protein from Escherichia coli. It shows amino-acid sequence similarity to human frataxin and a frataxin homologue in Saccharomyces cerevisiae, Yfh1p. The former is associated with the disease Friedreich ataxia and the latter plays a key role in iron homeostasis in mitochondria. CyaY has been overexpressed in soluble form in E. coli. The recombinant protein with a His(6) tag at its C-terminus has been crystallized at 296 K using polyethylene glycol (PEG) 4000 as a precipitant. Native diffraction data have been collected to 1.8 A using Cu Kalpha X-rays. The crystals belong to the trigonal space group P3(1)21 (or P3(2)21), with unit-cell parameters a = b = 44.66, c = 99.87 A, alpha = beta = 90.0, gamma = 120.0 degrees. The asymmetric unit contains one molecule of recombinant CyaY, with a corresponding V(m) of 2.13 A(3) Da(-1) and solvent content of 42.3%. |
| Links | |
| Keywords |
Bacterial Proteins/chemistry; Crystallization; Crystallography, X-Ray; Escherichia coli/chemistry; Escherichia coli Proteins; Humans; Iron-Binding Proteins; Phosphotransferases (Alcohol Group Acceptor)/chemistry; Protein Conformation; Recombinant Proteins/chemistry |
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