Matthew Byrne

University of Bristol

Papers

1

Total Citations

11

H-Index

1

About

Matthew Byrne is a structural biologist whose work centers on advancing protein crystallization techniques to unlock the three-dimensional structures of biomolecules. His most influential contribution is the development of random microseed matrix screening (rMMS), a powerful method that introduces seed crystals into random crystallization screens. This approach dramatically increases the likelihood of crystal growth by steering proteins into the metastable zone of their phase diagrams, yielding higher-quality crystals and additional crystallization leads. His landmark 2013 paper on rMMS has garnered 11 citations, reflecting its practical impact on the field. Byrne’s work is notable for addressing a persistent bottleneck in structural biology—the difficulty of obtaining diffraction-quality crystals—and for providing a robust, reproducible tool that researchers can readily adopt. By refining seeding strategies, he has helped accelerate the determination of protein structures, enabling deeper insights into biological function and drug design. His contributions are especially valuable for students and researchers seeking to overcome crystallization challenges, making him a key figure in the ongoing effort to visualize the molecular machinery of life.

Research Focus

Key Achievements

1
H-Index
1
Papers
11
Total Citations
11
Avg Citations/Paper
🏆 Most Cited Paper
Improving the Success Rate of Protein Crystallization by Random Microseed Matrix Screening
11 citations · 2013
📈 Most Prolific Year: 2013 (1 Papers)
🤝 Key Collaborators: 6
🏛 Institutions: University of Bristol

Top Papers

  1. 1

Key Collaborators

Contact & Links

Available for collaboration
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