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Richard Neutze

About Richard Neutze

Neutze’s group uses X-rays generated at synchrotrons and at X-ray free electron lasers to probe structural changes in membrane proteins. Membrane proteins are a very diverse class of proteins that control energy transduction and signalling processes in living organisms. By observing structural changes in membrane proteins we gain insight into how evolution has optimized them to perform chemical reactions essential for life. We have a strong history of international collaboration and we combine scientific questions with developing new methods to address these questions.

Neutze took his PhD in physics in 1995 from the University of Canterbury (New Zealand). He was introduced to the field of molecular biophysics by Janos Hajdu at Oxford University (England). Neutze accepted a Humboldt Fellowship in physics with Franz Hasselbäch at Tübingen University (Germany) before returning to molecular biophysics as a postdoc with Janos Hajdu at Uppsala University. In 1998 Neutze received an Assistant Professor grant from the Swedish Research Council. With this support Neutze relocated his group to Chalmers University of Technology in 2000. Six years later Neutze was appointed Professor of Biochemistry at the University of Gothenburg.

Nature Methods published an author profile on Richard Neutze which can be found here.

Important Publications

Photosynthetic reaction centres

Photosynthetic reaction centres harvest light to drive the charge-separation reactions that underpin photosynthesis, the major mechanism by which sunlight is converted into chemical energy in living cells. We have used time-resolved X-ray diffraction and time-resolved X-ray scattering to observe structural changes associated with these light-driven reactions.

R. Dods et al., Ultrafast structural changes within a photosynthetic reaction centre, Nature (2020).

D. Arnlund et al., Visualizing a protein quake with time-resolved X-ray scattering at a free-electron laser. Nature Methods 11, 923-926 (2014).

A.B. Wöhri et al., Light-induced structural changes in a photosynthetic reaction center caught by Laue diffraction, Science 328, 630-633 (2010).


Bacteriorhodopsin harvests light to pump protons across an energy transducing biological membrane, a second mechanism by which sunlight is converted into chemical energy in living cells. We have used time-resolved X-ray diffraction and low-temperature intermediate trapping to observe structural changes associated with these light-driven reactions.

P. Nogly et al., Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser. Science 361, eaat0094 (2018).

E. Nango et al., A three-dimensional movie of structural changes in bacteriorhodopsin. Science 354, 1552-1557 (2016).

M. Andersson et al., Structural dynamics of light driven proton pumps, Structure 17, 1265-75 (2009).

A. Royant et al., Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin, Nature 406, 645-648 (2000).

K. Edman et al. High resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle, Nature 401, 822-826 (1999).

Methodology developments using X-ray free electron lasers

X-ray free electron lasers were transformative technologies which increased the number of X-rays that could be focused onto a small-spot in a short time by a factor of a billion. We have pioneered new approaches utilizing these machines for structural studies of membrane proteins.

G. Brändén et al. Coherent diffractive imaging of microtubules using an X-ray laser, Nature Communications 10, 2589 (2019).

L.C. Johansson et al., Lipidic phase membrane protein serial femtosecond crystallography, Nature Methods 9, 263-265 (2012).

S. Boutet et al., High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography, Science 337, 362-364 (2012).

H. N. Chapman et al. Femtosecond X-ray protein nanocrystallography, Nature 470, 73-77 (2011).

R. Neutze et al., Potential for biomolecular imaging with femtosecond X-ray pulses, Nature 406, 752-757 (2000).

Structural studies of aquaporins

Aquaporins are membrane proteins that control the flow of water into and out of cells. We have used X-ray crystallography to reveal how the flow of water is regulated by eukaryotic aquaporins.

A. Frick et al., X-ray structure of human aquaporin 2 and its implications for nephrogenic diabetes insipidus and trafficking, PNAS 111,6305–6310 (2014).

U. Kosinska Eriksson et al., Sub-Ångstrom resolution x-ray structure details aquaporin-water interactions, Science 340, 1346-1349 (2013).

R. Horsefield et al. High resolution X-ray structure of human aquaporin 5, PNAS 105, 13327-13332 (2008).

S. Törnroth-Horsefield et al., Structural mechanism of plant aquaporin gating, Nature 439, 688-694 (2006).

Link to Google Scholar Page:

Citations and other metrics for Richard Neutze can be found here.


Neutze’s group is currently financed by Vetenskapsrådet (VR), the European Research Council (ERC) and Knut and Alice Wallenberg’s Foundation (KAW). Neutze has also previously received grants from the Swedish Strategic Research Foundation (SSF), various European Union funding frameworks (FP6, FP7, Horizon2020), Göran Gustafsson’s Foundation, and several other smaller funding bodies.