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Published September 2012 | Published
Journal Article Open

Crystallization and preliminary crystallographic studies of FoxE from Rhodobacter ferrooxidans SW2, an FeII oxidoreductase involved in photoferrotrophy

Abstract

FoxE is a protein encoded by the foxEYZ operon of Rhodobacter ferrooxidans SW2 that is involved in Fe^II-based anoxygenic photosynthesis (`photoferrotrophy'). It is thought to reside in the periplasm, where it stimulates light-dependent Fe^II oxidation. It contains 259 residues, including two haem c-binding motifs. As no three-dimensional model is available and there is no structure with a similar sequence, crystals of FoxE were produced. They diffracted to 2.44 Å resolution using synchrotron radiation at the Fe edge. The phase problem was solved by SAD using SHELXC/D/E and the experimental maps confirmed the presence of two haems per molecule.

Additional Information

© International Union of Crystallography. Received 22 June 2012; accepted 18 July 2012. The authors gratefully acknowledge the ESRF, Grenoble, France for provision of synchrotron radiation and thank Susana Gonçalves, ITQB–UNL, Portugal for diffraction data collection. G. M. Sheldrick is thanked for valuable discussions and for providing the SHELXE program. This work was funded by projects MIT-Pt/BS-BB/1014/2008 from the MIT-Portugal Program and PTDC/EBB-BIO/098352/2008 from FCT, Portugal. IHS is the recipient of a PhD grant from FCT (SFRH/BD/36582/2007). DKN is an HHMI Investigator.

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Created:
August 22, 2023
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