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About

J.A. Brannigan is a structural biologist whose research has centered on the high-throughput determination of protein structures from *Bacillus anthracis*, the bacterium responsible for anthrax. As a key contributor to the Structural Proteomics In Europe (SPINE) consortium, Brannigan helped pioneer a systematic, genomics-driven approach to solving protein structures from this medically important pathogen. Their most cited work, the crystal structure of dihydrodipicolinate synthase (BA3935) at 1.94 Å resolution (47 citations), provided atomic-level insight into an essential enzyme involved in bacterial cell wall synthesis. Brannigan also elucidated the structure of PurE (BA0288), an enzyme critical for nucleotide biosynthesis, and co-authored a landmark paper (27 citations) describing the application of high-throughput technologies to structural proteomics of *B. anthracis*. By combining crystallography with bioinformatics and automated pipeline methods, Brannigan’s work has not only advanced our understanding of anthrax pathogenesis but also demonstrated how structural genomics can rapidly deliver functional insights for biodefense and drug discovery. Their contributions remain a foundation for researchers targeting essential bacterial proteins.