Publications by authors named "M Shelby"

Article Synopsis
  • - Chlamydia is a widespread bacterial STD that often goes unnoticed, creating a need for a preventive vaccine to address its serious health risks.
  • - Cell-free protein synthesis (CFPS) allows for quick and adaptable production of vaccine proteins, demonstrated by producing the chlamydial CT584 protein for testing in mice.
  • - Although CT584 prompted strong antibody responses, it failed to effectively protect against chlamydia infection, highlighting CFPS's potential for producing other antigens even if this candidate wasn't successful.
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Article Synopsis
  • Counter diffusion is a superior method for growing large, high-quality protein crystals compared to traditional techniques, producing better diffraction data and structures.
  • The article presents user-friendly designs for counter-diffusion chambers in a 2D microfluidic chip, allowing for efficient crystal growth and preservation.
  • This innovative approach maintains crystal hydration for extended periods, simplifies chip fabrication using common materials, and enhances crystallography capabilities by minimizing sample handling and background scatter.
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is the most prevalent bacterial sexually transmitted pathogen worldwide. Since chlamydial infection is largely asymptomatic with the potential for serious complications, a preventative vaccine is likely the most viable long-term answer to this public health threat. Cell-free protein synthesis (CFPS) utilizes the cellular protein manufacturing machinery decoupled from the requirement for maintaining cellular viability, offering the potential for flexible, rapid, and de-centralized production of recombinant protein vaccine antigens.

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Serial crystallography at large facilities, such as x-ray free-electron lasers and synchrotrons, evolved as a powerful method for the high-resolution structural investigation of proteins that are critical for human health, thus advancing drug discovery and novel therapies. However, a critical barrier to successful serial crystallography experiments lies in the efficient handling of the protein microcrystals and solutions at microscales. Microfluidics are the obvious approach for any high-throughput, nano-to-microliter sample handling, that also requires design flexibility and rapid prototyping to deal with the variable shapes, sizes, and density of crystals.

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The development of x-ray free electron laser (XFEL) light sources and serial crystallography methodologies has led to a revolution in protein crystallography, enabling the determination of previously unobtainable protein structures and near-atomic resolution of otherwise poorly diffracting protein crystals. However, to utilize XFEL sources efficiently demands the continuous, rapid delivery of a large number of difficult-to-handle microcrystals to the x-ray beam. A recently developed fixed-target system, in which crystals of interest are enclosed within a sample holder, which is rastered through the x-ray beam, is discussed in detail in this Perspective.

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