Hi All, I'm thinking of embarking on some crystallisation of a membrane protein in bicelles in the new year. In the methods I've read you simply take your protein in detergent and add the bicelle mxiture (Chapso+DMPC) to your protein allow the solution to equilibrate and set up your screens. What I was wondering is will the original concentration of detergent in your protein sample, effect the likelihood of crystallization (i.e. by changing the structure of the bicelle)? If so do people generally seek to minimize the detergent concentration of the sample before setting up the bicelles.
Cheers, Rhys
