Seiki Kuramitsu
Papers
2
Total Citations
31
H-Index
2
About
Seiki Kuramitsu is a pioneering structural biologist whose work has fundamentally advanced our understanding of thermophilic proteins through the lens of structural genomics. His primary research focuses on the structure and function of proteins from the extreme thermophile *Thermus thermophilus* HB8, an organism whose heat-stable proteins are ideal for crystallographic studies. Kuramitsu’s major contribution lies in developing the high-throughput crystallization infrastructure essential for the whole-cell structural project on *T. thermophilus* HB8. His landmark 2008 paper, cited 29 times, describes the systematic screening and robotic setup—using HTS-80, Crystal Finder, and TERA robots—that enabled efficient crystallization of hundreds of proteins, setting a gold standard for thermophilic structural genomics. Among his notable achievements is the 2004 crystal structure determination of the conserved hypothetical protein TT1751, which, despite its modest citation count, exemplifies his commitment to elucidating the function of uncharacterized proteins from this model organism. Kuramitsu’s work has provided a robust platform for the community, enabling countless downstream studies on protein stability, evolution, and drug design. His legacy is a comprehensive structural encyclopedia of a thermophilic bacterium, demonstrating how systematic, high-throughput approaches can unlock the secrets of life at extreme temperatures.
Research Focus
Key Achievements
Top Papers
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