Thank you all.
I think i have known the reason for the low occupancy.
First, I co-crystallized the protein and peptide with a molar ratio 1:5. In
this situation, the peptide likely would fully occupy the protein binding
site. But the crystal is hard to freezen, so stepwise freezen method was
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Dear All:
Thank you for help. Now I will make a summary of this topic.
First, the actual situation is that:
1. Protein and peptide have a affinity about 10E-7 to 10E-8 molar.
2. The 2.6 angstrom data were got from a co-crystal and had a wilson B about
70, in the experiment protein/peptide have a
