Wolfram Saenger

Wolfram Saenger
Born1939
Known forX-ray crystallography of membrane proteins
AwardsGottfried Wilhelm Leibniz Prize, Humboldt Prize
Scientific career
FieldsBiochemistry and protein crystallogtaphy
InstitutionsMax Planck Institute for Experimental Medicine, Harvard Medical School, Free University of Berlin, National Academy of Sciences

Wolfram Saenger (born 1939) is a German biochemist and protein crystallographer. In his research career spanning over 30 years he has worked at the Max Planck Institute for Experimental Medicine, Harvard University (Harvard Medical School) and the Free University of Berlin, where he led the Institute for Crystallography research until his retirement in 2011. A recipient of the Gottfried Wilhelm Leibniz Prize (1987) of the Deutsche Forschungsgemeinschaft, which is the highest honor awarded for achievements in research in Germany, and the Humboldt Prize (1988), he is best known for his research on X-ray crystallography of membrane proteins and protein-nucleic acid complexes. He has authored 10 books, including the venerated book 'Principles of Nucleic Acid Structure' published by Springer, and over 500 scientific articles.

He is a fellow of the National Academy of Sciences.

Partial list of major scientific contributions

  1. Water Molecule in Hydrophobic Surroundings: Structure of alpha-Cyclodextrin-Hexahydrate (C6H10O5)6·6H2O, Nature, 1972
  2. Circular hydrogen bonds, Nature, 1979
  3. Specific protein-nucleic acid recognition in ribonuclease T1−2'-guanylic acid complex: an X-ray study, Nature 1982
  4. DNA conformation is determined by economics in the hydration of phosphate groups, Nature 1986
  5. Long-range structural changes in proteinase K triggered by calcium ion removal, Nature 1989
  6. Three-dimensional structure of the E. coli DMA-binding protein FIS, Nature 1991
  7. Three-dimensional structure of system I of photosynthesis at 6 Å resolution, Nature 1993
  8. Crystal structure of beta-D-cellotetraose hemihydrate with implications for the structure of cellulose II, Science 1994
  9. Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance, Science 1994
  10. Characterization of non-inducible Tet repressor mutants suggests conformational changes necessary for induction, Nature Structural Biology 1995
  11. Photosystem I at 4 Å resolution represents the first structural model of a joint photosynthetic reaction centre and core antenna system, Nature Structural Biology 1996
  12. Structural basis of gene regulation by the tetracycline inducible Tet repressor− operator system, Nature Structural Biology 2000
  13. Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution, Nature 2001
  14. Three-dimensional structure of cyanobacterial Photosystem I at 2.5 Å resolution, Nature 2001
  15. Towards complete cofactor arrangement in the 3.0 Å resolution structure of photosystem II, Nature 2005
  16. Where water is oxidized to dioxygen: structure of the photosynthetic Mn4Ca cluster, Science 2006
  17. Cyanobacterial photosystem II at 2.9 Å resolution and the role of quinones, lipids, channels and chloride, Nature Structural & Molecular Biology 2009