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Updated: Jun 21, 2026

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

Self-assembly-induced protein crystallization.

Hongjun Liu¹, Sanat K Kumar, Jack F Douglas

¹Department of Chemical Engineering, Columbia University, New York, New York 10027, USA.

Physical Review Letters

|August 8, 2009

Summary

This summary is machine-generated.

Transient protein clusters, even outside thermodynamic stability, can drive crystal nucleation. The patchy nature of protein interactions facilitates self-assembly, guiding crystal formation and morphology.

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Area of Science:

Biophysics
Materials Science
Computational Chemistry

Background:

Protein clusters within liquid-liquid coexistence regions are known to promote crystal nucleation.
Recent experimental findings suggest protein nucleation can occur outside these phase boundaries.
Understanding the mechanisms of protein self-assembly and nucleation is crucial for controlling crystallization.

Purpose of the Study:

To investigate protein nucleation and crystal growth facilitated by transient clusters formed outside thermodynamic stability.
To explore the role of anisotropic interprotein interactions in protein self-assembly and nucleation.
To model protein crystallization using a minimal patchy particle system.

Main Methods:

Simulated a minimal model of patchy particles representing anisotropic interprotein interactions.
Investigated cluster formation and subsequent crystal nucleation under various thermodynamic conditions.
Analyzed the influence of particle patchiness on self-assembly and crystal morphology.

Main Results:

Transient protein clusters can nucleate crystal growth even when a dense protein liquid is thermodynamically unstable.
The patchy nature of interactions significantly enhances protein self-assembly.
Self-assembled clusters guide the morphology of the resulting protein crystals.

Conclusions:

Protein self-assembly into transient clusters is a key mechanism for nucleation, extending beyond traditional liquid-liquid coexistence boundaries.
Anisotropic interactions, modeled by patchy particles, are critical for facilitating this self-assembly and subsequent crystal formation.
This work provides insights into controlling protein crystallization through understanding interprotein interactions and self-assembly dynamics.