Hey Amit,

as your protein is tiny, maybe you can calculate a molecular replacement model as described in Acta Cryst. (2009). D65, 169–175.

This might take longer than engineering a few methionines, though. I'd mutate leucines.


Andreas



amit sharma wrote:
Dear All,

I have a 9-kDa protein that crystallizes well. Since there is no structural homologue for this molecule, I intend to make Se-Met derivative of the protein. The molecule has no Met/Cys residues in its sequence. I wanted to know where in the sequence should I mutate, so that the folding/crystallizability of the protein is not compromised.

Any suggestions would be of great help.

Thanks in advance,
--
Amit Sharma, Ph.D. Research Associate, Department of Biology,
University of York, YO10 5DD UK

--
        Andreas Förster, Research Associate
        Paul Freemont & Xiaodong Zhang Labs
Department of Biochemistry, Imperial College London

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