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Updated: May 18, 2026
On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature
Published on: March 11, 2022
Crystallization and preliminary crystallographic studies of FoxE from Rhodobacter ferrooxidans SW2, an Fe(II)
L Pereira1, I H Saraiva, R Coelho
1Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Apartado 127, 2781-901 Oeiras, Portugal.
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.
