Hi All, I'm currently working of a protein with a ferredoxin protein with anIron-Sulphur cluster. I was harvesting some crystals the other day and a piece of my scalpel blade broke off and ended up in the well solution. I Sealed the well without noticing, the shard of iron oxidised and the crystals lost most of their red colour:
Ordinary crystals: http://s1058.photobucket.com/albums/t401/__Rhys__/?action=view¤t=MBPR_Rodcluster2edit.png Crystals from Blade containing well: http://s1058.photobucket.com/albums/t401/__Rhys__/?action=view¤t=MBPR_Bleached.png My explanation for this (If someone has a different one that'd be great too) Is that the oxidation of the metallic iron the well, created reducing conditions in the chamber and reduced the iron-sulphur cluster (reduced ferredoxin is much less strongly coloured). Which got me to thinking...Could this be applied as a technique to create reducing conditions in protein crystallography, as the use of reducing agents isn't always practical. Cheers, Rhys Grinter PhD Candidate University of Glasgow
