Hi guys,
What are the routine methods by which you generate terminal truncations
of a protein of interest for subsequent screening for purification,
stability and efficient folding for the purposes of crystallization?
My protein has 2 known domains and a conserved C-terminal part which is
defined as domain by sequence homology with other proteins. We would
like to generate different lengths of the protein containing this
C-terminus and screen them for expression, solubility, purification, and
folding and thus increase our chances for success.
appreciate all help
Iva
