Have you looked at a UV-vis scan, there are some characteristic bumps you should see depending on the state of your FeS cluster, plus you can monitor if oxidation occurs over time. If I remember it correctly 322 nm is where you want to look at.
Jürgen On Jul 11, 2012, at 6:22 AM, Jan Rashid Umar wrote: Dear All, I will be grateful to your suggestions about Iron-Sulfur cluster protein purification. My colleague has some problems with the purification and it seems that the iron-sulfur cluster might be deformed, and protein is aggregated. The purification is done under aerobic (normal condition), and is there some method to reintegrate iron sulfur cluster back into the protein molecule under these conditions. Can anybody suggest some literature, protocol or something that can improve the protein aggregation? I look forward to hearing from you. Best wishes, Jan ...................... Jürgen Bosch Johns Hopkins University Bloomberg School of Public Health Department of Biochemistry & Molecular Biology Johns Hopkins Malaria Research Institute 615 North Wolfe Street, W8708 Baltimore, MD 21205 Office: +1-410-614-4742 Lab: +1-410-614-4894 Fax: +1-410-955-2926 http://lupo.jhsph.edu
