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].
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).
To investigate the contribution of specific restrictocin−SRL contacts from the RNA side, variants that included multiple mutations were used rather than point mutants.
Because several of the point mutants decreased but did not abolish transcriptional reporter activity in multiple cells, selected combinatorial point mutants were generated and tested in SW480 cells.
Point mutants of xtGadd45a, were obtained by circular PCR [32].
