Rather than looking at "anti-DTT" it is more important to set up an appropriate redox system. This can be a combination of reduced and oxidised glutathione or cysteine. If you check some of the commercial protein refolding screens this should give you an idea about relative concentrations.
Best regards, Paul.. ------------------------------------------------------------------------ ----------------- Dr. Paul A. McEwan Senior Scientist (Structural Biology) Evotec (UK) Ltd. 114 Innovation Drive | Milton Park | Abingdon | Oxfordshire | OX14 4SA email: [email protected] <mailto:[email protected]> Tel: +44 (0)1235 861561 Fax:+44 (0)1235 863139 direct line: +44 (0)1235 838802 www.evotec.com <http://www.evotec.com> From: CCP4 bulletin board [mailto:[email protected]] On Behalf Of Jacob Keller Sent: 28 February 2013 11:09 To: [email protected] Subject: Re: [ccp4bb] disulfide engineering Along these lines, what reagents do people use to promote disuflide bonds, i.e., the "anti-DTT?" JPK On Thu, Feb 28, 2013 at 2:06 AM, David Briggs <[email protected]> wrote: You might want to try "Disulfide by design" http://cptweb.cpt.wayne.edu/DbD2/ Cheers Dave On Feb 28, 2013 6:55 AM, "Careina Edgooms" <[email protected]> wrote: Dear CCP4 members I wish to engineer a disulfide bond at the dimer interface of a protein I am working with. Does anyone know of any available software to assist with this? Best Careina -- ******************************************* Jacob Pearson Keller, PhD Postdoctoral Associate HHMI Janelia Farms Research Campus email: [email protected] ******************************************* Evotec (UK) Ltd is a limited company registered in England and Wales. Registration number:2674265. Registered office: 114 Milton Park, Abingdon, Oxfordshire, OX14 4SA, United Kingdom.
