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Growth of Diffraction-Quality Protein Crystals Using a Harvestable Microfluidic Device
Michael J Y Lee1, Frédérick Faucher1, Zongchao Jia1
1Department of Biomedical and Molecular Sciences, Queen's University , Kingston, Ontario K7L 3N6, Canada.
Crystal Growth & Design
|July 12, 2014
Summary
Microfluidic devices called Crystal Formers streamline protein crystallography. This study successfully used a Crystal Former to rapidly obtain diffraction-quality crystals of the Legionella pneumophila protein LidL for structure determination.
Area of Science:
- Structural Biology
- Biophysics
- Molecular Biology
Background:
- Protein crystallography is essential for determining protein structures but often faces significant bottlenecks in crystal formation.
- Traditional high-throughput screening methods for protein crystallization can be time-consuming and costly.
- Microfluidic devices offer a promising alternative for efficient and rapid crystallization screening.
Purpose of the Study:
- To evaluate the efficacy of commercially available microfluidic Crystal Former devices for protein crystallization.
- To demonstrate the application of Crystal Formers in obtaining diffraction-quality crystals for structure determination.
- To optimize crystal screening for the Legionella pneumophila protein LidL.
Main Methods:
- Utilized a 96-channel Crystal Former microfluidic device for screening protein crystallization conditions.
- Applied the Crystal Former to crystallize the protein LidL from Legionella pneumophila.
- Collected X-ray diffraction data from the obtained crystals.
Main Results:
- Successfully obtained a diffraction-quality crystal of the LidL protein using a single Crystal Former tray setup.
- The crystal diffracted X-rays to a resolution of 2.76 Å.
- Demonstrated the time- and cost-saving potential of Crystal Formers in protein crystallography.
Conclusions:
- Crystal Former microfluidic devices are effective tools for rapid and efficient protein crystallization screening.
- This technology can significantly reduce the time and cost associated with obtaining crystals for structure determination.
- The successful crystallization of LidL highlights the utility of Crystal Formers for challenging proteins.
