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About

Karl Harlos has made pioneering contributions to structural biology, particularly in high-throughput protein crystallography and the structural analysis of immune receptors. His key research areas include developing robotic crystallization methods and determining protein structures from pathogenic organisms. Harlos co-developed a seminal procedure for setting up nanolitre-scale crystallization experiments, achieving 100 nl vapour-diffusion sitting drops; his 2003 paper on this system, cited over 130 times, demonstrated its day-to-day reliability across more than 50 unrelated protein samples, revolutionizing early-stage crystallization trials. He also led a high-throughput structural proteomics project on *Bacillus anthracis*, the anthrax-causing pathogen, collaborating with SPINE partners to accelerate structure determination of biomedically relevant targets. Additionally, Harlos contributed to the systematic production and structural analysis of soluble αβ T-cell receptors, providing insights into immune recognition. His work has enabled faster, more efficient protein structure determination, impacting drug discovery and vaccine development. With over 170 citations across his most-cited works, Harlos is recognized for advancing automation in structural biology and for his role in unlocking the structures of challenging proteins.