Temperature dependence of protein solubility — determination and application to crystallization in X-ray capillaries

Rosenberger, Franz; Howard, Sandra B.; Sowers, Jennifer W.; Nyce, Thomas A.

doi:10.1016/0022-0248(93)90427-x

Cited by 152 publications

(115 citation statements)

References 39 publications

Supporting

Mentioning

102

Contrasting

Unclassified

Order By: Relevance

“…The higher solubility at lower temperature, "retrograde" temperature dependence of solubility (Rosenberger et al, 1993), is similar to the one known for deoxy-HbS , and has been encountered with many other proteins (McPherson, 1982;1999).…”

Section: Concentrationsupporting

confidence: 54%

“…Over the last 15 years the solubility of lysozyme and in particular its tetragonal crystals has been studied by several groups, employing a variety of techniques (Ataka & Asai, 1988;Howard et al, 1988;Miyashita et al, 1993;Ries-Kautt & Ducruix, 1989;Rosenberger et al, 1993). Fortunately, in the areas of overlap, these techniques have produced rather consistent results, certifying to the accuracy of the determinations (Miyashita et al, 1993;Rosenberger et al, 1993).…”

Section: Lysozyme -Negative Crystallization Enthalpy and Entropymentioning

confidence: 99%

See 1 more Smart Citation

Solvent entropy contribution to the free energy of protein crystallization

Vekilov

Feeling-Taylor²,

Yau³

et al. 2002

Acta Crystallogr D Biol Crystallogr

102

View full text Add to dashboard Cite

We show with three proteins that trapping and release of the water molecules upon crystallization is a determinant of the crystallization thermodynamics. With HbC, a strong retrograde solubility dependence on temperature yields a high positive enthalpy of 155 kJ mol -1 , i.e., crystallization is only possible because of the huge entropy gain of 610 J mol, stemming from the release of up to 10 water molecules per protein intermolecular contact. With apoferritin, the enthalpy of crystallization is close to zero. The main component in the crystallization driving force is the entropy gain due to the release upon crystallization of two water molecules bound to one protein molecules in solution. With both proteins, the density of the growth sites imaged by AFM is in excellent agreement with a calculation using the crystallization free energy. With lysozyme, the entropy effect due to the restructuring of the water molecules is negative. This leads to higher solubility.

show abstract

Section: Concentrationsupporting

confidence: 54%

Section: Lysozyme -Negative Crystallization Enthalpy and Entropymentioning

confidence: 99%

Solvent entropy contribution to the free energy of protein crystallization

Vekilov

Feeling-Taylor²,

Yau³

et al. 2002

Acta Crystallogr D Biol Crystallogr

102

View full text Add to dashboard Cite

show abstract

“…We note that such an entropic attraction is not contained in DLVO theory. Its origin is also different from the salting out effect studied in [12,[57][58][59][60] or the macroion overcharging effect studied in [61]. In Figure 8 the salt dependence of the total interaction force F (r) (Eq.…”

Section: Microion Distributions Around a Single Proteinmentioning

confidence: 83%

Nonmonotonic variation with salt concentration of the second virial coefficient in protein solutions

et al. 2003

View full text Add to dashboard Cite

The osmotic virial coefficient B 2 of globular protein solutions is calculated as a function of added salt concentration at fixed pH by computer simulations of the "primitive model". The salt and counter-ions as well as a discrete charge pattern on the protein surface are explicitly incorporated. For parameters roughly corresponding to lysozyme, we find that B 2 first decreases with added salt concentration up to a threshold concentration, then increases to a maximum, and then decreases again upon further raising the ionic strength.Our studies demonstrate that the existence of a discrete charge pattern on the protein surface profoundly influences the effective interactions and that nonlinear Poisson Boltzmann and Derjaguin-Landau-Verwey-Overbeek (DLVO) theory fail for large ionic strength. The observed non-monotonicity of B 2 is compared to experiments. Implications for protein crystallization are discussed.

show abstract

“…Using this method, they determined a saturation equilibrium point within 24 hours. Rosenberger et al (1993) developed a scintillation method for determining the temperature dependence of the solubility, and of nucleation induction times of proteins in 50-100 /il volumes of solution in a space of a few hours. They used the data for the controlled separation of the nucleation and growth stages by changing the temperature when nucleation was observed (by means of light scattering).…”

Section: Solubility and Phase Diagramsmentioning

confidence: 99%

Trends and Challenges in Experimental Macromolecular Crystallography

Chayen

Boggon

Cassetta

et al. 1996

Quart. Rev. Biophys.

View full text Add to dashboard Cite

Macromolecular X-ray crystallography underpins the vigorous field of structural molecular biology having yielded many protein, nucleic acid and virus structures in fine detail. The understanding of the recognition by these macromolecules, as receptors, of their cognate ligands involves the detailed study of the structural chemistry of their molecular interactions. Also these structural details underpin the rational design of novel inhibitors in modern drug discovery in the pharmaceutical industry. Moreover, from such structures the functional details can be inferred, such as the biological chemistry of enzyme reactivity. There is then a vast number and range of types of biological macromolecules that potentially could be studied. The completion of the protein primary sequencing of the yeast genome, and the human genome sequencing project comprising some 105 proteins that is underway, raises expectations for equivalent three dimensional structural databases.

show abstract

Temperature dependence of protein solubility — determination and application to crystallization in X-ray capillaries

Cited by 152 publications

References 39 publications

Solvent entropy contribution to the free energy of protein crystallization

Solvent entropy contribution to the free energy of protein crystallization

Nonmonotonic variation with salt concentration of the second virial coefficient in protein solutions

Trends and Challenges in Experimental Macromolecular Crystallography

Contact Info

Product

Resources

About