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You know the sequence of the target so the missing residues can be built by looking at the difference density. if the protein is phased right by MR then the extra residues if they were actually present (and not clipped off in crystallization) you should see them. coot can be used to visualize and build residues by build loop or baton mode. if you have a bulky residue say phenylalanine then that will definitely be a land mark to go forward in building.

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Karthik
Graduate Student
University of Michigan

On Sat, Oct 31, 2009 at 8:02 AM, rui <[log in to unmask]> wrote:
Dear All,

I have a question about how to find missing density or fill gap. I'm trying to use MR to solve a crystal structure that diffract to 2.6A. The target sequence has extra residues than the template sequence,say from residues 20 to 26. Now how can I insert those extra residues? At this moment, my solution has the same number of residues as the template and it's hard to see extra densities. Should I delete some residues before and after the loop first then try to bring up the missing densities?Any suggestions would be appreciated. Thanks.

Rui