Thanks to All for the diligent answers to my query, The protein is not thermophilic and has only one cysteine. We are working in presence of freshly added reducing agent and glycerol to promote solubility (well kinda it seems). This is not an RNA or DNA binding protein and it has no low-complexity regions except at the N terminus, there maybe some left over from a cryptic transit peptide (somehow basic) that supposedly targets the protein to a specific organelle. We are probably going to truncate further to see if it solves our problem
I appreciate all the comments and suggestions, Cheers, Pascal -- Pascal F. Egea, PhD Assistant Professor UCLA, David Geffen School of Medicine Department of Biological Chemistry Boyer Hall room 356 611 Charles E Young Drive East Los Angeles CA 90095 office (310)-983-3515 lab (310)-983-3516 email pe...@mednet.ucla.edu
