Using a Microfluidic Device for Protein Crystallization
Author Information
Author(s): Vivian Stojanoff, Jean Jakoncic, Deena A. Oren, V. Nagarajan, Jens-Christian Navarro Poulsen, Melanie A. Adams-Cioaba, Terese Bergfors, Morten O. A. Sommer
Primary Institution: National Synchrotron Light Source, Brookhaven National Laboratories
Hypothesis
Can a microfluidic device improve the identification of crystallization conditions for proteins compared to traditional methods?
Conclusion
The microfluidic Crystal Former significantly increases the number of identified crystallization conditions compared to vapour diffusion methods.
Supporting Evidence
- The Crystal Former yielded crystals for 5%, 28%, and 8% of conditions for thaumatin, catalase, and myoglobin, respectively.
- In contrast, sitting-drop vapour diffusion had success rates of only 1%, 7%, and 1% for the same proteins.
- 90% of the crystals grown in the Crystal Former were unique and not identified by the sitting-drop method.
Takeaway
Scientists used a special device to help grow protein crystals better than before, making it easier to study them.
Methodology
Crystallization trials were performed using both the Crystal Former and sitting-drop vapour-diffusion plates to compare the effectiveness of each method.
Potential Biases
Potential conflicts of interest due to authors' employment with companies involved in the technology.
Limitations
The study primarily focused on a limited number of proteins and conditions, which may not represent all crystallization scenarios.
Digital Object Identifier (DOI)
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