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David G. Waterman is a structural biologist whose work bridges high-throughput structural proteomics and computational methods for macromolecular crystallography. His key research areas include pathogen biology, particularly the structural characterization of proteins from *Bacillus anthracis*, and the development of advanced software for X-ray diffraction data analysis. Waterman made major contributions to the structural proteomics of anthrax, leading a collaborative SPINE project that applied high-throughput technologies to determine structures of proteins from this biomedically critical pathogen. His most cited paper (27 citations) describes this pioneering effort to rapidly solve structures of *B. anthracis* proteins, providing a foundation for understanding anthrax pathogenesis and potential therapeutic targets. Beyond this, Waterman is widely recognized for his work on the DIALS and Xia2 software packages, which have become essential tools for the global crystallography community, enabling automated, robust data processing. His impact is reflected in the widespread adoption of these computational tools, which have transformed how diffraction data are analyzed. Waterman’s combination of experimental structural biology and software development has made him a key figure in modern structural biology, facilitating discoveries across numerous biological systems.