Measuring Protein Solubility

  • Neer AsherieEmail author
Part of the Methods in Molecular Biology book series (MIMB, volume 2039)


Protein solubility determines the conditions under which the protein will remain in solution. As a result, it is an important quantity in applications that involve concentrated protein solutions. Here I describe the solubility measurement of the protein thaumatin in the presence of tartrate ions as a function of temperature. This method can be used to measure the solubility of other proteins.

Key words

Protein Solubility Thaumatin Protein crystallization Phase diagrams 



I gratefully acknowledge financial support from the National Science Foundation (DMR 0901260 and 1206416) and Yeshiva University.


  1. 1.
    McPherson A (1999) Crystallization of biological macromolecules. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NYGoogle Scholar
  2. 2.
    McManus JJ, Charbonneau P, Zaccarelli E, Asherie N (2016) The physics of protein self-assembly. Curr Opin Colloid Interface Sci 22:73–79CrossRefGoogle Scholar
  3. 3.
    Trevino SR, Scholtz JM, Pace CN (2008) Measuring and increasing protein solubility. J Pharm Sci 97:4155–4166CrossRefGoogle Scholar
  4. 4.
    Benvenuti M, Magnani S (2007) Nat Protoc 2:1633–1651CrossRefGoogle Scholar
  5. 5.
    McPherson A, Gavira JA (2014) Introduction to protein crystallization. Acta Crystallogr F Struct Biol Commun 70(Pt 1):2–20CrossRefGoogle Scholar
  6. 6.
    Astier J-P, Veesler S (2008) Using temperature to crystallize proteins: a mini-review. Cryst Growth Des 8:415–4219CrossRefGoogle Scholar
  7. 7.
    Aldabeideh N, Jones MJ, Myerson AS, Ulrich J (2009) The solubility of orthorhombic lysozyme crystals obtained at high pH. Cryst Growth Des 9:3313–3317CrossRefGoogle Scholar
  8. 8.
    Berland CR, Thurston GM, Kondo M, Broide ML, Pande J, Ogun O, Benedek GB (1992) Solid-liquid phase boundaries of lens protein solutions. Proc Natl Acad Sci U S A 89:1214–1218CrossRefGoogle Scholar
  9. 9.
    Sleutel M, Willaert R, Gillespie C, Evrard C, Wyns L, Maes D (2009) Kinetics and thermodynamics of glucose isomerase crystallization. Cryst Growth Des 9:497–504CrossRefGoogle Scholar
  10. 10.
    Feeling-Taylor AR, Banish RM, Hirsch RE, Vekilov PG (1999) Miniaturized scintillation technique for protein solubility determinations. Rev Sci Instrum 70:2845–2849CrossRefGoogle Scholar
  11. 11.
    Rowe JB, Cancel RA, Evangelous TD, Flynn RP, Pechenov S, Subramony JA, Zhang J, Wang Y (2017) Metastability gap in the phase diagram of monoclonal IgG antibody. Biophys J 113:1750–1756CrossRefGoogle Scholar
  12. 12.
    Ko TP, Day J, Greenwood A, McPherson A (1994) Structures of three crystal forms of the sweet protein thaumatin. Acta Cryst D 50:813–825CrossRefGoogle Scholar
  13. 13.
    Asherie N, Ginsberg C, Blass S, Greenbaum A, Knafo S (2008) Solubility of thaumatin. Cryst Growth Des 8:1815–1817CrossRefGoogle Scholar
  14. 14.
    Asherie N, Ginsberg C, Greenbaum A, Blass S, Knafo S (2008) Effect of protein purity and precipitant stereochemistry on the crystallization of thaumatin. Cryst Growth Des 8:4200–4207CrossRefGoogle Scholar
  15. 15.
    Asherie N (2004) Protein crystallization and phase diagrams. Methods 34:266–272CrossRefGoogle Scholar

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© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Department of PhysicsYeshiva UniversityNew YorkUSA
  2. 2.Department of BiologyYeshiva UniversityNew YorkUSA

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