Petra Fromme

Petra Fromme
Petra Fromme
Arizona State University
Department of Chemistry and Biochemistry
P.O. Box 871504
Tempe, AZ 85287-1504
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(480) 965-9028
With over 20 years of experience in the field of membrane protein X-ray crystallography, Dr. Fromme's expertise lies in fs crystallography and developmental methodology for the structural determination of membrane proteins. Specifically, this methodology is related to X-ray structure analysis based on hundred-thousands of X-ray diffraction patterns from a stream of fully hydrated nano/microcrystals of membrane protein crystals. Dr. Fromme's lab was the first to crystallize and unravel structural questions related to Photosystem I and II. This breakthrough was significant, as Photosystem I (consisting of 36 proteins and 381 cofactors non-covalently bound) are the most complex membrane proteins to have their structural makeup determined. In addition, to the Photosystems, the Fromme Lab studies the structures of ATP synthase, as well as membrane proteins involved in infectious diseases.

Dr. Fromme is Director and Principal Investigator of the MPID (Membrane Proteins in Infectious Diseases) Center, one of nine National Institute of Health-funded PSI Biology Centers. In this role, Dr. Fromme spearheads research for the development of methodology for the structure determination of membrane proteins. The MPID is also engaged in research related to the function of protein complexes utilizing spectroscopic methods (both in solution and single crystals), including Electron Paramagnetic Resonance (EPR) and ultrafast spectroscopy.

The Fromme Lab's undertakings in the BioXFEL Center will include: continuing its focus upon fs crystallography methodology and exploring biological queries utilizing novel methodology; developing improved methods for sample delivery that work in high throughput with minimal sample use; developing methodology for evaluation of nanocrysatllography data (including development of new algorithms for indexing and structure factor refinement, as well as phase determination); developing time-resolved methodology for fs nanocrystallography, enzymatic reaction in biology (utilizing photo-labile substrates) and of membrane cell structure protein receptors upon binding of the effector molecule.