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Preparation and Delivery of Protein Microcrystals in Lipidic Cubic Phase for Serial Femtosecond Crystallography
Published on: September 20, 2016
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Supersaturation-controlled microcrystallization and visualization analysis for serial femtosecond crystallography.
Dan Bi Lee1, Jong-Min Kim2, Jong Hyeon Seok1
1Department of Biotechnology & Bioinformatics, Korea University, Sejong, Korea.
Scientific Reports
|February 9, 2018
Summary
Researchers developed accessible microcrystallization methods and tools for X-ray Free Electron Laser (XFEL) studies. This technique enables high-density protein microcrystal formation, crucial for observing fast biological reactions.
Area of Science:
- Structural Biology
- Biophysics
- Crystallography
Background:
- Time-resolved serial femtosecond crystallography using X-ray Free Electron Lasers (XFELs) offers a powerful method for studying fast reactions at near-physiological temperatures.
- A significant challenge hindering widespread XFEL adoption is the difficulty in producing and characterizing homogeneous, high-density, micron-sized protein crystals in standard laboratories.
Purpose of the Study:
- To develop and present accessible microcrystallization techniques and associated visualization/analysis tools suitable for any laboratory setting.
- To overcome the bottleneck of protein crystal production for XFEL studies, thereby democratizing access to this advanced structural biology method.
Main Methods:
- Development of supersaturation-controlled microcrystallization in a vapor diffusion mode, utilizing controlled evaporation of hanging drops (30 seconds to 3 minutes).
- Optimization of microcrystallization conditions, initially for influenza virus hemagglutinin, by employing rapid evaporation techniques.
- Creation of visualization and analysis tools for characterizing microcrystals observed via light microscopy, enabling assessment of size and density distributions.
Main Results:
- Successful application of supersaturation-controlled microcrystallization to generate high-density microcrystals of lysozyme, ferritin, and hemagglutinin.
- Demonstration that the developed visualization and analysis tools provide accurate microcrystal characterization, consistent with manual analysis and high-resolution microscopy.
- The methods significantly improve reproducibility in microcrystal formation compared to initial attempts.
Conclusions:
- The presented supersaturation-controlled microcrystallization technique and associated tools provide a universally accessible solution for producing protein microcrystals.
- These advancements are expected to significantly facilitate and broaden the scope of X-ray Free Electron Laser (XFEL) studies in structural biology.
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