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A high throughput platform for eukaryotic genes.

Yunjia Chen1, Shihong Qiu, Chi-Hao Luan

  • 1Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL, USA.

Methods in Molecular Biology (Clifton, N.J.)
|June 11, 2008
PubMed
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A high-throughput pipeline was developed for structural proteomics to accelerate the determination of protein structures and fold families. This automated system efficiently handles numerous samples, aiding in the analysis of protein structures.

Area of Science:

  • Structural proteomics
  • Biochemistry
  • Molecular biology

Background:

  • Structural proteomics aims to map all protein structures and fold families.
  • High-throughput (HTP) methods are crucial for accelerating structural biology research.
  • Developing efficient pipelines is essential for large-scale protein structure determination.

Purpose of the Study:

  • To establish a HTP cloning and expression pipeline for structural proteomics.
  • To automate the production and analysis of a large number of recombinant proteins.
  • To create a public resource for organizing and analyzing protein structures and fold families.

Main Methods:

  • Utilized Gateway cloning/expression technology for recombinant protein production.
  • Implemented a stepwise automation strategy on an integrated robotic platform.

Related Experiment Videos

  • Developed a pipeline capable of processing up to 384 unique samples in parallel.
  • Automated processes from PCR to protein solubility profiling.

    • Main Results:

    • Successfully developed and implemented a HTP pipeline for structural proteomics.
    • The automated system efficiently handles gene cloning and protein expression analysis.
    • The pipeline demonstrated parallel processing of up to 384 unique samples.
    • Achieved automation of key steps including PCR and protein solubility profiling.

    Conclusions:

    • The developed HTP pipeline significantly advances structural proteomics research.
    • Automated, parallel processing enhances the efficiency of recombinant protein production and analysis.
    • This approach facilitates the creation of comprehensive protein structure and fold family resources.