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Gerlind Sulzenbacher is a structural biologist whose work has significantly advanced the field of structural genomics, particularly through the development of high-throughput crystallization methodologies. Her research focuses on determining the three-dimensional structures of proteins of unknown function, with a key emphasis on bacterial proteins from organisms like *E. coli*. Her major contribution is pioneering a medium-throughput crystallization approach (2002, 80 citations), which demonstrated the power of combining robotic screening with manual optimization to solve protein structures efficiently. This methodology has become a cornerstone for large-scale structural biology projects. Sulzenbacher’s notable work includes solving the crystal structure of the *E. coli* yddE protein (2004), revealing a striking homology with diaminopimelate epimerase—an enzyme critical for bacterial cell wall biosynthesis. This discovery provided functional insights into previously uncharacterized proteins, showcasing the value of structural genomics in linking sequence to biological function. Her achievements highlight the importance of automation and systematic approaches in accelerating structural determination, making her a key figure in the transition from traditional crystallography to modern, high-throughput pipelines.