Academic Appointments

  • Research Engineer, Bioengineering

Boards, Advisory Committees, Professional Organizations

  • Member, Department of Structural Biology DEI Committee (2021 - Present)

Contact

  • Academic
    cltarver@stanford.edu
    University - Academic staff Department: Program-Chiu, W. Position: Research Engineer

Additional Info

  • Mail Code: 5126
  • SUNet ID(s):
    cltarver

All Publications

  • Ionic Liquids as Protein Crystallization Additives. Crystals Tarver, C. L., Yuan, Q., Pusey, M. L. 2021; 11 (10)

    Abstract

    Among its attributes, the mythical philosopher's stone is supposedly capable of turning base metals to gold or silver. In an analogous fashion, we are finding that protein crystallization optimization using ionic liquids (ILs) often results in the conversion of base protein precipitate to crystals. Recombinant inorganic pyrophosphatases (8 of the 11 proteins) from pathogenic bacteria as well as several other proteins were tested for optimization by 23 ILs, plus a dH2O control, at IL concentrations of 0.1, 0.2, and 0.4 M. The ILs were used as additives, and all proteins were crystallized in the presence of at least one IL. For 9 of the 11 proteins, precipitation conditions were converted to crystals with at least one IL. The ILs could be ranked in order of effectiveness, and it was found that ~83% of the precipitation-derived crystallization conditions could be obtained with a suite of just eight ILs, with the top two ILs accounting for ~50% of the hits. Structural trends were found in the effectiveness of the ILs, with shorter-alkyl-chain ILs being more effective. The two top ILs, accounting for ~50% of the unique crystallization results, were choline dihydrogen phosphate and 1-butyl-3-methylimidazolium tetrafluoroborate. Curiously, however, a butyl group was present on the cation of four of the top eight ILs.

    View details for DOI 10.3390/cryst11101166

    View details for PubMedID 34745654