Dear ccp4
Apologies for the off topic question. I was wondering whether anyone could suggest a good tool or methodology to use to predict protein solubility and ability to fold from the sequence? I am working with a large protein of multiple domains. I would like to work with as close to the full length protein as possible without affecting its solubility and ability to fold correctly. I know there are web based tools where you can upload a sequence and see the predicted solubility but I wonder if there is any good strategy to use to determine how best to construct the truncated protein? ie which parts of the sequence to keep and which to remove so as to maximise solubility. Also I have an eye to crystallising this protein in the future and I wonder if there are any specific things I should look out for with that in mind? I'm sure minimising flexible loops is one such thing. All help appreciated Best Careina
