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Orthorhombic lysozyme solubility.

F Ewing1, E Forsythe, M Pusey

  • 1Science and Technology Corporation, Madison, AL 35758, USA.

Acta Crystallographica. Section D, Biological Crystallography
|July 1, 1994
PubMed
Summary
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The high-temperature orthorhombic form of chicken egg-white lysozyme exhibits lower temperature sensitivity than the tetragonal form. Its solubility decreases with increasing pH, unlike the low-temperature form.

Area of Science:

  • Biochemistry
  • Crystallography
  • Protein Science

Background:

  • Chicken egg-white lysozyme exists in different crystalline forms.
  • The orthorhombic form is stable at higher temperatures (above 298 K).
  • Understanding lysozyme solubility is crucial for crystallization and protein studies.

Purpose of the Study:

  • To determine the solubility diagrams for the orthorhombic form of chicken egg-white lysozyme.
  • To compare the solubility behavior of the orthorhombic form with the previously studied tetragonal form.
  • To investigate the effects of temperature, pH, and precipitant concentration on orthorhombic lysozyme solubility.

Main Methods:

  • Micro-column technique used for solubility determination.
  • Solubility data collected across a pH range of 4.0 to 5.4.

Related Experiment Videos

  • Experiments conducted within a temperature range of 297 K to 317 K.

    • Main Results:

    • Orthorhombic lysozyme solubility increases with temperature and decreases with precipitant concentration.
    • Solubility of the orthorhombic form shows less temperature sensitivity compared to the tetragonal form.
    • Solubility of the orthorhombic form decreases with increasing pH, opposite to the tetragonal form.

    Conclusions:

    • The orthorhombic form of lysozyme has distinct solubility characteristics compared to the tetragonal form.
    • Phase diagrams reveal differences in temperature and pH dependencies.
    • Combined data provide insights into lysozyme's phase behavior under varying conditions.