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Dialysis

Dialysis

Dialysis is a diffusion-based purification process that separates analyte molecules from a complex matrix. This is accomplished by allowing molecules in the solution to pass through a semipermeable membrane into a liquid on the other side. The membrane is usually made of cellulose acetate or cellulose nitrate, and the second liquid must be miscible with the solution. Ions (e.g., chloride or sodium) or organic molecules (e.g., glucose) can pass through the membrane pores, which generally have...

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Related Experiment Video

Updated: Mar 19, 2026

High-Throughput Protein Crystallization via Microdialysis

High-Throughput Protein Crystallization via Microdialysis

Published on: March 3, 2023

A crystallization apparatus for temperature-controlled flow-cell dialysis with real-time visualization.

Niels Junius¹, Esko Oksanen¹, Maxime Terrien¹

¹Université Grenoble Alpes, IBS, F-38044 Grenoble, France; CNRS, IBS, F-38044 Grenoble, France; CEA, IBS, F-38044 Grenoble, France.

Journal of Applied Crystallography

|June 9, 2016

Summary

This study introduces a novel apparatus for rational protein crystal growth optimization. It enables precise control over temperature and precipitant concentration, improving crystal size and diffraction quality for structural biology.

Keywords:

dialysis macromolecular crystallography optimization of crystal growth phase diagrams temperature control

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Last Updated: Mar 19, 2026

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Published on: March 3, 2023

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Published on: April 11, 2021

Area of Science:

Structural Biology
Biophysics
Materials Science

Background:

Current crystallization methods prioritize high-throughput screening over optimizing crystal growth.
Improving crystal size and diffraction quality requires decoupling nucleation and growth, which is challenging with existing parallel assays.
Existing setups struggle to control critical parameters like precipitant concentration, equilibration rate, and temperature.

Purpose of the Study:

To develop an integrated apparatus for rational optimization of protein crystal growth.
To enable precise control and manipulation of temperature-precipitant concentration phase diagrams.
To improve crystal size, morphology, and diffraction quality for structural studies.

Main Methods:

Development of a temperature-controlled dialysis button integrated into a novel apparatus.
Serial experimentation approach exploring multiple conditions with a single protein sample.
Utilizing dialysis with a flowing precipitant reservoir and precise temperature control for reversible condition manipulation.
Software for real-time visualization and control of temperature and solution composition.

Main Results:

Demonstrated a method for rational optimization of crystal growth, moving beyond initial condition screening.
Successfully mapped and manipulated temperature-precipitant concentration phase diagrams.
Achieved tailored crystal size, morphology, and diffraction quality.
Significantly reduced the time, effort, and protein material required for structure determination.

Conclusions:

The developed apparatus and strategy offer a paradigm shift from parallel to serial experiments for crystal growth optimization.
This approach allows for efficient and reversible exploration of crystallization conditions.
The rational optimization strategy enhances the quality of protein crystals, facilitating structural biology research.