D. Holzle
Papers
1
Total Citations
19
H-Index
1
About
D. Holzle is a structural biologist whose work centers on elucidating the three-dimensional architecture of proteins from pathogenic bacteria, with a particular focus on uncharacterized or hypothetical proteins. Their most significant contribution is the determination of the crystal structure of the YfiH protein from *Shigella flexneri*, a pathogen responsible for bacillary dysentery. Using the single-wavelength anomalous dispersion (SAD) method, Holzle solved this structure at an impressive 2.01 Å resolution, providing the first detailed view of a member of a vast, conserved protein family. This foundational work, published in 2006, has garnered 19 citations, serving as a critical reference for researchers exploring the function of YfiH homologs across different species. By illuminating the shape and fold of this previously enigmatic protein, Holzle’s research has opened new avenues for understanding bacterial physiology and identifying potential targets for therapeutic intervention. Their meticulous approach to structural genomics highlights the power of X-ray crystallography in decoding the molecular machinery of life, making a lasting impact on the field of microbial structural biology.
Research Focus
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Top Papers
- 1