Hi Sam, Depends on your problem. If the cysteins are alone and exposed and is not involved in multimeric assemly, adding reducing agent helps in keeping the them(monomers) from non productive association that hinders crystallization.
On the other hand if they support multimer formation which is physiological, then it might be more sane to not use reducing agents. Another worth a penny try is, if you have homology model, try to see if the cysteins in the same crystal setting helps to form crystal lattice in the homology model. If yes, then it maybe useful to try not use the reducing agents in crystallization. If No, try otherwise. With this in mind you can expand your trials to get your optimum reducer concentration. Just my thoughts; may/maynot be useful ! best Natesh. On Fri, 27 Jun 2008, Sam wrote: > Date: Fri, 27 Jun 2008 14:44:02 +0100 > From: Sam <[EMAIL PROTECTED]> > To: [email protected] > Subject: [ccp4bb] Reducer and crystallization > > Dear all, > > Can anyone enlighten me the effect of reducer in crystallography? > I understand that it removes disulphide bond, and prevent protein > aggregation. But how do we find a balance point and must we remove it before > screening crystals? > > Thanks for answering first. > > > Cheers > sam > ------------------------------------- Failures are more finely etched in our minds than triumphs, and success is an elusive, if not mythic, goal in our demanding society (Hugh Drummond). ------------------------------------- Ramanathan Natesh Wellcome Trust Advanced Training Fellow School of Crystallography Birkbeck College University of London Malet Street London WC1E 7HX Tel: +44 (0)20-7631-6835 Fax: +44 (0)20-7631-6803
