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The B-factor method doesn't seem to be a good method for the GPCRs. Likely this is because the transmembrane helices are so tightly bound that automatically the rest of the protein is much more flexible. It is known that making mutations in the transmembrane helices can make GPCRs more stable. This is nicely demonstrated by the "thermostability" literature search. Clearly the two methods do not overlap indicating that the B-factor method does not apply to GPCRs. It is in this protein family probably much better to first try the positions that are already published to have an effect on the stability. The best way to do this is to find amino acids described in literature that are know known to stabilize GPCRs. If the stabilizing residue is not in your target GPCR then it might be a good idea to try that residue. If your target sequence has a different residue than the consensus it might be smart to try the consensus residue as there are several papers demonstrating that making the consensus often has a beneficial effect on the stability. (Note that if it is easy to screen your protein for thermostability than randomizing each hotspot might be smarter). There are many other tricks too. Here are some examples: 

1. Introducing prolines at positions where a proline is common and your target doesn't have a proline
2. Inserting negative charges at the N side of a helix (if there isn't any). Or a positive residue at the C-side. This is known as helix capping because the N terminus of a helix is slightly positive and the C-terminus is slightly negative.
3. Creating salt-bridges by inserting positive or negative residues at positions on the outside of the protein. Always check if the residue you want to use is actually common in the alignment at that position.
4. Replacing glycines where, according to the alignment, glycines can be replaced by something else.