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Each construct in the mutation library was tested for full-length TAS2R16 translation and surface expression by immunofluorescent antibody binding assays.

The entire TAS2R16 mutation library was transfected into human HEK-293T cells in a 384-well array format (one clone per well) and evaluated for salicin-dependent activation measured by a calcium flux assay (Fig. 1a).

Four amino acid residues (L17, F119, L167, and L266) in the hydrophobic substrate-binding pocket of the lipase were selected for mutation based on a structural model of a substrate enzyme complex, and a combinatorial mutation library was constructed by SIMPLEX and screened for (R) and (S -configurations of p-nitrophenyl 3-phenylbutyrate.

These data indicate that the mutation library was successfully constructed.

ENU induced mutation library was screened for a mutation in the fmr1 gene.

The mutation library was validated using new and publically available sequence and phenotypic data from 792 isolates, from six countries (Canada, China, Malawi, Pakistan, Portugal and Russia; see Additional file 1: Table S3).

After removal of such duplicated mutations, the mutation density in the library was estimated as at least 15.7 mutations per 1 kb from the number of unique 18 mutations in the 1144-bp region.

Concentrations for mutation library screening were chosen to be approximately 2 to 3 times higher than the EC50 values for the ligands to maximize the sensitivity of detecting decreases in signaling due to the mutation in each clone.

Having assessed the diagnostic potential of the mutation library, comparison was made with the polymorphisms used in commercially available molecular tests for drug resistance.

An N‐ethyl‐ N‐nitrosourea (ENU) mutagenized library was screened for mutations in exons 3, 4, 5, 6, and 7, encoding the kinase domain of the zebrafish pink1 homologue.

Concentrations chosen for mutation library screening were approximately 2 to 3 times higher than the EC50 value for each ligand to maximize the sensitivity of detecting decreases in signaling due to the mutation in each clone (3 mM salicin, 5 mM hexyl-β-glucoside, 1.6 mM 4-NP-β-mannoside, and 10 mM β-glucosaminide).