Hi all, Just to mention a side-comment relevent to Prasenjit's question:
Considering the prevalence of synchrotron-radiation-damaged disulfides, well documented in the literature, it seems that all disulfides in proteins whose data were collected at synchrotron sources should be modeled with two conformations. Therefore, if there is not an easy way to do this now, we should try to implement a good way to do this in the future. All the best, Jacob Keller ==============Original message text=============== On Fri, 06 Jul 2007 12:46:29 pm CDT Prasenjit Bhaumik wrote: Hello, We are trying to refine a structure using REFMAC and we are facing problem in refining the double conformations of a cysteine residue. One conformation is involved in formation of a disulfide linkage and other conformation is free. Is there any way to define the restraints so that both the conformations can be refined. With kind regards, Prasenjit -- Prasenjit Bhaumik, Ph.D. Protein Structure Section Macromolecular Crystallography Laboratory National Cancer Institute at Frederick 1050 Boyles Street, Building-539, Room-145 P.O. Box B, Frederick, MD-21702, USA Phone: 301-846-1974, Fax: 301-846-7101 E-mail: [EMAIL PROTECTED] ------------------------------------------------- ===========End of original message text=========== *********************************** Jacob Keller Northwestern University 6541 N. Francisco #3 Chicago IL 60645 (847)467-4049 [EMAIL PROTECTED] ***********************************
