The Murphy Lab

The Murphy Lab

Max-Planck Research Group

We are an independent Max Planck Research Group based at the MPI of Biophysics in Frankfurt. We work to discover the structure and mechanism of proteins, mostly proteins of bioenergetic relevance, using single-particle cryo-EM.

Understanding mechanism through structure

As a new independent group at the Max Planck Institute of Biophysics, our goal is to understand, at an atomic level, the function of sophisticated proteins that mediate the chemistry of life. Our focus is on metalloproteins, especially redox proteins, and the bioenergetic and regulatory processes that they mediate. Our core technique is single-particle cryo-EM, a versatile and powerful tool that allows us to determine structures of protein complexes at atomic or near-atomic resolutions, without the need to grow crystals. At least as important as the static structure, however, are the dynamics of the protein complexes, which are closely linked to function. Due to the relatively flexible nature of cryo-EM sample preparation, combined with an ability to separate mixed populations of different conformational states in silico, this toolkit gives us an unprecedented ability to understand mechanism through the lens of structure.

Our work is built upon a foundation of biochemical and molecular biology techniques. We have recently set up a plunge-freezing device in an anaerobic tent, which allows control of the gas atmosphere under which cryo-EM sample grids are prepared and frozen. This has allowed us to obtain high-resolution structures of oxygen-sensitive proteins, and to use the gas composition to control redox potential for some proteins. We are actively building on this in order to fully control the redox potential of cryo-EM samples up to the point of freezing.

We do not currently have any advertised positions. Candidates interested in working in the group should send a CV and letter of motivation to Bonnie Murphy.

Selected Publications

Murphy B.J., Klusch N., Langer J., Mills D.J., Yildiz Ö., et al.  
Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F1-Fo coupling.
Science 364. (2019)
Klusch N., Murphy B.J., Mills D.J., Yildiz Ö., Kühlbrandt W.
Structural basis of proton translocation and force generation in mitochondrial ATP synthase.
Elife 6 (2017).
Murphy B.J., Hidalgo R., Roessler M.M., Evans R.M., Ash P.A., et al.
Discovery of Dark pH-Dependent H(+) Migration in a [NiFe]-Hydrogenase and Its Mechanistic Relevance: Mobilizing the Hydrido Ligand of the Ni-C Intermediate.
J Am Chem Soc 137: 8484–8489 (2015).
McDowall J.S., Murphy B.J., Haumann M., Palmer T., Armstrong F.A., et al.
Bacterial formate hydrogenlyase complex.
Proc Natl Acad Sci USA 111: E3948-56 (2014).
Murphy B.J., Sargent F., Armstrong F.A.
Transforming an oxygen-tolerant [NiFe] uptake hydrogenase into a proficient, reversible hydrogen producer.
Energy Environ Sci 7: 1426 (2014).

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