rfromme

Raimund Fromme

Assoc Research Professor
School of Molecular Sciences
Faculty Member
Applied Structural Discovery

Location: TEMPE

Contact Information
Raimund.Fromme@asu.edu
(480) 727-4749

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,    73?77.

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 Macromolecular diffractive imaging using imperfect crystals

Pande et al.(2016) Science 352, 725-729,  DOI: 10.1126/science.aad5081

 

Bio

Raimuch Fromme's research has investigated the inner sanctum of photosynthesis, the structure and function of Photosystem I and II, since is master's and doctorate work. Since 2004, he has had the opportunity to work on crystal structures of various proteins in the broad field of photosynthesis, where the membrane proteins are the most interesting and challenging proteins of all. 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 unknown. 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 II or the photoactive yellow protein(PYP).