Hi All, I'm currently working on solving the structure of a protein by molecular replacement. The protein is around 30kDa and likely has a two beta-prism domains, linked by a long curved two stranded sheet based on the structure of an analogue. There are also a number of other structures which represent a single homologous beta-prism domain. I've tried to find MR solution using the analogue and various truncation/AA substitution models based on it with no success. I've also tried single domain ensembles of the other homologous structures, also with no success. I think the problem is the overall sequence homology is quite low between my protein and the available structures (35% for the analogue and around 20% for the other models.
I was curious as to how someone with more experience would tackle this problem. Just for background, the datasets I have are 2 to 2.7 angstroms with pretty nice stats. The space group is most likely C2221 with two molecules per ASU (giving around 58% solvent). Thanks, Rhys Grinter PhD Candidate University of Glasgow
