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This ambiguity derives from the fact that studies suggesting DHIPK2-mediated phosphorylation of Ser-297 of Gro were based on the use of a multiple point mutant in which Ser-297 was mutated together with Ser-194, Ser-196, Ser-285, and Ser-287 [29].
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OX2 multiple point mutants were generated in the C-terminus using site-directed mutagenesis to replace serine and threonine residues with alanine.
We focused on the mutant fitness distribution and obtained the optimal mixing ratio which efficiently generates superior multiple-point mutants with high fitnesses.
Our method handles single- and multiple-point mutants in the same manner.
We have assembled the largest such dataset as yet, consisting of of 137 single- and multiple-point mutants along with data on changes to their solubilities.
In fact, it may be more accurate on multiple-point mutants, as the number of triplets involved in the mutation will typically be larger.
By exploring the literature, we have assembled a structural dataset of 137 single- and multiple-point mutants along with the associated increases or decreases in the wild-type (WT) solubilities.
This nodulation phenotype was observed in the SACPD-C deletion lines A6, MM106 (data not shown) and FN8-10, as well as multiple, independent the point mutant lines; i.e. 194D (V211E), KK24 (C298Δ) and FAM94-41 (D126N).
Both of the Sox17 truncations and the point mutant maintained the ability to interact with Smad3 across multiple binding stringencies (Fig. 7C).
CTMP point mutant (m5) was generated by site-directed mutagenesis.
A point mutant in this latter gene was obtained (fur1).
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