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[ccp4bb]: Selenomethionine oxidation during RP-HPLC

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Dear all,

I'd like to purify a small disulphide-rich protein containing
selenomethionine for MAD on a C8 reverse phase column. The buffers I
normally use contain 0.1% TFA and Acetonitrile and are purged with helium,
but the disulphide bonds in my protein don't allow me to use a reducing
agent such as DTT or beta-mercaptoethanol. If anyone has had to deal with
a similar case before, could they please let me know whether the
selenomethionine became chemically modified during this purification step.

Best regards,