Sentence examples for mutants were purified from inspiring English sources

The soluble fractions of these mutants were purified by hydrophobic, gel filtration and ion-exchange column chromatography.

These mutants were purified and screened for binding, yielding a map of residues that are required for binding and a complementary map of residues that are not required.

All proteins, except the TAM mutants, were purified as described in Garforth et al.[5].

Finally, minichromosomes containing the H1.4 domain mutants were purified and visualised with the AFM (Figure S3).

The S177D and S177E mutants were purified as described for the wildtype His-tagged MEP synthase.

Recombinant His6-eIF4AIII and mutants were purified through a Ni++-NTA agarose (Qiagen) column as previously described [33].

To test this hypothesis, the kinase domain from each of the suppressor mutants was purified from bacteria and tested as a substrate for YopJ in an in vitro acetylation reaction.

Given that the Ca6 site mutants are purified with lower yields, this site is likely important for protein folding.

Bacterial lysate expressing GST-Snail proteins (WT, ΔZF and ZF mutants) was purified by immobilization on glutathione Sepharose beads (Pharmacia Biotech/GE Healthcare, Uppsala, Sweden).

His-tagged MptpB WT and mutants was purified by standard nickel affinity chromatography on a 5 ml HiTrap column (Amersham Bioscience) in binding buffer (50 mM Hepes, 500 mM NaCl, pH 7) and eluted 300 mM imidazole.

His-tagged proteins (CG9523 and its mutant) were purified using Ni2+ affinity purification (Qiagen) and were aliquoted at stored at −80°C in 20 mM Tris, pH 7.5, 5 mM NaCl, 1 mM DTT, and 10% glycerol.