rfromme
Raimund Fromme
Location: TEMPE
Education
Ph.D. Chemistry, Technical University of Berlin 1994
Research Interests
The inner sanctum of Photosynthesis the structure and function of Photosystem I and II is since my master thesis and PhD the focus of my research interest. Since 2004 I have the opportunity to work on crystal structures of various proteins in the broad field of photosynthesis. The membrane proteins are the most interesting and challenging proteins at all. Currently the protein data bank has above 150,000 structures, in contrast the number of known unique membrane protein structures is still around 850 . Therefore the most important proteins are in their majority still unknown by their structure, beside the fact that the numeric share is around one third of all proteins. The field of membrane protein structure determination is still in the beginning with a clear growing impact to many research topics in chemistry, biochemistry, biology and medicine. Diffraction with the X-ray femtosecond Free Electron Laser(FEL) is the newest tool to provide information about the dynamic change of structures like photosystem II or the photoactive yellow protein(PYP).
Article I have been corresponding author :
Gisriel et al. (2017) Science accepted July 28 online
Articles I contributed as co author:
Chapman et al. (2011) Nature 470, 7377.
Boutet et al.(2012) Science 337(6092):362-4.
Redecke et al. (2013) Science 339(6116):227-30
Liu et al. (2013) Science 20 December 2013: 1521-1524
Kupitz et al. (2014) Nature 9 July doi:10.1038/nature13453
Tenboer et al. (2014) Science 5 December : 1242-1246. [DOI:10.1126/science.1259357]
Kang et al. (2015) Nature doi:10.1038/nature14656, online 22 July 2015
Ayyer et al. (2016) Nature, 530, 202-206
Pande et al.(2016) Science 352, 725-729, DOI: 10.1126/science.aad5081
Bio
Raimund Fromme's research has investigated the inner sanctum of photosynthesis, the structure and function of Photosystem I and II, since his master's and doctorate work. Beginning in 2004, he has had the opportunity to work on crystal structures of various proteins. His main focus are the membrane proteins, the most interesting and challenging proteins. Currently the protein data bank has more than 150,000 structures, in contrast the number of known unique membrane protein structures, which hovers around 850. This means that the structure of some of the most important proteins are in their majority (one third of all proteins) still remain undetermined. For this reason the field of membrane protein structure determination is still in its beginnings, with a clear growing impact on many research topics in chemistry, biochemistry, biology and medicine. Diffraction with the X-ray femtosecond Free Electron Laser(FEL) is the newest tool to provide information about the dynamic change of structures like photosystem I or II and many other proteins.