Dear All,

Sorry for an offtopic question, your suggestions are highly appreciated.

We have been working on iron sulfur cluster binding protein, which is
usually expressed as a nice soluble protein expressed in BL21 cells but
aggregated in the affinity column itself and unable to recover from it. We
had made n number of truncations and fused to soluble tags such as MBP, but
always ended up in large aggregates. Anyone has experience in working with
iron-sulfur cluster binding protein before, please let us know the critical
steps in purification of such proteins, whether you have completely done
the expression, purification and crystallization in anaerobic conditions?
or else changing the expression system to eukaryotic system such as Baculo
or HEK 293T would help?

Please share your valuable experience, thank you.



-- 
Best Regards,
Umar Farook

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