Protein crystallization in confined geometries
S. Tanaka, S. U. Egelhaaf, W. C. K. Poon
TL;DR
This study investigates how confinement within lipid cubic phases affects protein crystallization, revealing a significant decrease in lysozyme solubility due to spatial restrictions, supported by experiments and simulations.
Contribution
It demonstrates that confinement in lipid cubic phases reduces protein solubility, providing insights into protein crystallization in confined geometries.
Findings
Lysozyme solubility decreases by a factor of ~4 in cubic phase.
Confinement explains the reduced solubility through spatial restriction.
Simulations support experimental observations.
Abstract
We studied the crystallization of a globular protein, lysozyme, in the cubic phase of the lipid monoolein. The solubility of lysozyme in salt solution decreased by a factor of when confined in cubic phase. Calculations and Monte Carlo simulations show that this can be explained by the {\it confinement} of lysozyme molecules to the narrow water cells in the cubic phase.
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Taxonomy
TopicsLipid Membrane Structure and Behavior · Protein Structure and Dynamics · Crystallization and Solubility Studies