Hello, We can make a nice 1:1 complex between two proteins that then gradually precipitates during storage at 4 degC. With 0.005% Tween-20 the complex is stable and does not preciptate noticeably. We have used this in buffers to measure the kinetics of binding by Biacore so it is clearly compatible with "functionality".
Is Tween-20 at this concentration compatible with crystallisation? Is it worth giving a go, or a waste of time? Should we try and remove it, or reprepare the complex in an alternative detergent? If we need to try an alternative, what would people recommend? Thanks in advance for your suggestions, Darren -- ********************************************************************** Dr. Darren Hart, Team Leader High Throughput Protein Lab Grenoble Outstation European Molecular Biology Laboratory (EMBL) ********************************************************************** EMBL webpages: http://tinyurl.com/6xdltl http://tinyurl.com/667jrp Email: h...@embl.fr Tel: +33 4 76 20 77 68 Fax: +33 4 76 20 71 99 Skype: hartdarren Postal address: EMBL, 6 rue Jules Horowitz, BP181, 38042 Grenoble, Cedex 9, France **********************************************************************
