On 24/01/07, Peter Adrian Meyer <[EMAIL PROTECTED]> wrote:
> We have crystallized a 21KD protein with 2 disulfide bonds grown for one > month in 0.1M tri-sodium citrate pH 5.6, 0.5M (NH4)2SO4 and 1M Li2SO4. The > crystals look big (~0.4mm x 0.4mm x 0.3mm) and pretty (sharp edge, clean > surface) but diffracted to only 4A in-house. The spots are quite strong > and isotropic at low resolution but decay sharply beyond 5-6A. The crystal Have you tried DTT (or another way of keeping things in a reducing environment)? This might help keep your disulfides (and hopefully protein) happy.
Surely the addition of a _reducing_ agent would _reduce_ your disulphides - i.e. break them. Dave Pete
Pete Meyer Fu Lab BMCB grad student Cornell University
-- --------------------------------------- David Briggs, PhD. Father & Crystallographer www.dbriggs.talktalk.net iChat AIM ID: DBassophile
