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Related Experiment Video

Updated: Apr 22, 2026

$On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature$

On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature

Published on: March 11, 2022

Room-temperature serial crystallography using a kinetically optimized microfluidic device for protein crystallization

Michael Heymann¹, Achini Opthalage², Jennifer L Wierman³

¹Graduate Program in Biophysics and Structural Biology, Brandeis University, 415 South Street, Waltham, MA 02454, USA ; Martin Fisher School of Physics, Brandeis University, 415 South Street, Waltham, MA 02454, USA.

|October 9, 2014

Summary

A new emulsion-based serial crystallography method enables single crystal analysis from nanoliter droplets. This technique successfully determined the glucose isomerase structure, paving the way for high-throughput protein structure determination.

Keywords:

X-ray diffraction microfluidic devices protein crystallization serial crystallography

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$Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography$

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography

Published on: April 24, 2018

Area of Science:

Structural Biology
Biophysics
Crystallography

Background:

Serial crystallography is a powerful technique for determining protein structures.
Traditional methods face challenges with crystal handling and data collection.

Purpose of the Study:

To develop an emulsion-based serial crystallography technology for efficient data collection.
To demonstrate the feasibility of high-throughput structure determination using this novel method.

Main Methods:

Nanoliter protein solution droplets were encapsulated in oil and stabilized by surfactant.
A negative feedback mechanism was utilized to achieve one crystal per droplet.
Diffraction data were collected from room-temperature crystals on a microfluidic chip.

Main Results:

A 93% complete diffraction data set was obtained by merging single frames from multiple crystals.
The structure of glucose isomerase was solved to a resolution of 2.1 Å.
The method demonstrated high-throughput serial X-ray crystallography using synchrotron radiation.

Conclusions:

The developed emulsion-based serial crystallography technology is feasible for protein structure determination.
This approach offers a promising avenue for high-throughput structural biology studies.
The technique advances the capabilities of X-ray crystallography for analyzing challenging protein targets.