A. Joachimiak

Joint Center for Structural Genomics, Argonne National Laboratory

Papers

Total Citations

231

H-Index

About

A. Joachimiak is a leading figure in structural genomics, whose work has fundamentally advanced our understanding of protein architecture through high-throughput crystallography. As a key contributor to the NIH-NIGMS Protein Structure Initiative, Joachimiak helped pioneer the large-scale determination of protein structures, with seminal papers like "High-throughput crystallography for structural genomics" (114 citations) and "Contributions to the NIH-NIGMS Protein Structure Initiative from the PSI Production Centers" (65 citations) establishing the methodological and operational frameworks for this field. His research has yielded critical insights into pathogen biology, most notably the crystal structure of *Bacillus anthracis* transpeptidase CapD (33 citations), which revealed the molecular mechanism by which the anthrax pathogen anchors its protective capsule to the cell wall—a finding with direct implications for developing anti-infective therapies. Joachimiak has also solved structures of previously uncharacterized proteins, such as the hypothetical protein YfiH from *Shigella flexneri* (19 citations), demonstrating the power of structural genomics to illuminate function from form. Through these contributions, Joachimiak has not only expanded the structural encyclopedia of life but also provided a blueprint for how high-throughput methods can accelerate discovery in both basic biology and infectious disease research.