Richard Neutze

Professor of Biochemistry

Department of Chemistry & Molecular Biology

University of Gothenburg

 

Telephone:   +46 31 7863974 

E-mail: This e-mail address is being protected from spambots. You need JavaScript enabled to view it.

Curriculum Vitae

Publications




Bibliography

Richard Neutze received his PhD in physics in 1995 from the University of Canterbury, New Zealand. He did a short postdoc with Janos Hajdu at the Department of Molecular Biophysics, Oxford University, prior to accepting a Humboldt Fellowship with Franz Hasselbach at the Department of Applied Physics, Tübingen University. In 1997 he rejoined the group of Janos Hajdu, which had relocated to the Department of Biochemistry, Uppsala University. In 1998 Richard received an Assistant Professorship from the Swedish Research Council, which enabled him to move to Chalmers University of Technology in 2000. In 2006 Richard accepted a Professorship of Biochemistry at The University of Gothenburg.

Research

Richard Neutze received his PhD in physics in 1995 from the University of Canterbury, New Zealand. He did a short postdoc with Janos Hajdu at the Department of Molecular Biophysics, Oxford University, prior to accepting a Humboldt Fellowship with Franz Hasselbach at the Department of Applied Physics, Tübingen University. In 1997 he rejoined the group of Janos Hajdu, which had relocated to the Department of Biochemistry, Uppsala University. In 1998 Richard received an Assistant Professorship from the Swedish Research Council, which enabled him to move to Chalmers University of Technology in 2000. In 2006 Richard accepted a Professorship of Biochemistry at The University of Gothenburg.

Research

For more than a decade our research has focussed on membrane protein structure and structural dynamics probed using synchrotron radiation and x-ray free electron lasers.

Scientific highlights include solving x-ray structures of plant, yeast and human aquaporins1-3. These structures revealed molecular details concerning how post-translational regulation of aquaporins occurs in eukaryotes.

We used x-ray crystallography to study retinal proteins (bacteriorhodopsin; sensory rhodopsin II; proteorhodopsin) in their resting4 and intermediate states trapped at low temperature5-7. We have developed the method of time-resolved wide angle x-ray scattering (TR-WAXS) to probe structural changes in retinal proteins at room temperature in real time8,9. We also helped explore the functional role of retinal proteins in oceanic bacteria.10

We have applied similar techniques to probe structural changes in bacterial photosynthetic reaction centres: both trapped at low temperature11 and using time-resolved Laue diffraction at room temperature12. These reaction centres have also proven useful systems for developing lipid rich approaches to membrane protein crystallisation.13

We proposed that ultra-fast, ultra-intense diffraction would create revolutionary new possibilities for extracting structural information from very small biological samples14. We have helped demonstrate this concept – called diffraction before destruction – in ultrafast protein nano-crystallography studies at the LCLS, the world’s first X-ray free electron laser15. We have extended this approach – coined serial femtosecond crystallography - to extract structural information from membrane protein crystals grown in a lipidic sponge phase.16 This method has been extended to high-resolution studying nano-crystals of soluble proteins.17,18  

 

Difference Fourier map (laser on minus laser off) calculated from a time-resolved Laue diffraction study, showing a light induced movement of TyrL162 towards the special pair three milliseconds after photoactivation.


 

References

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

2              Horsefield, R. et al. High-resolution x-ray structure of human aquaporin 5. Proc Natl Acad Sci U S A 105, 13327-13332 (2008).

3              Fischer, G. et al. Crystal structure of a yeast aquaporin at 1.15 angstrom reveals a novel gating mechanism. PLoS Biol 7, e1000130 (2009).

4              Royant, A. et al. X-ray structure of sensory rhodopsin II at 2.1-A resolution. Proc Natl Acad Sci USA 98, 10131-10136 (2001).

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

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

7              Edman, K. et al. Early structural rearrangements in the photocycle of an integral membrane sensory receptor. Structure 10, 473-482 (2002).

8              Andersson, M. et al. Structural dynamics of light-driven proton pumps. Structure 17, 1265-1275 (2009).

9              Westenhoff, S. et al. Rapid readout detector captures protein time-resolved WAXS. Nature Methods 7, 775-776 (2010).

10           Gómez-Consarnau, L. et al. Light stimulates growth of proteorhodopsin-containing marine Flavobacteria. Nature 445, 210-213 (2007).

11           Katona, G. et al. Conformational regulation of electron transfer rates in a photosynthetic bacterial reaction centre. Nature Structural Molecular Biology 12, 630-631 (2005).

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

13           Johansson, L. C., Wohri, A. B., Katona, G., Engstrom, S. & Neutze, R. Membrane protein crystallization from lipidic phases. Curr Opin Struct Biol 19, 372-378 (2009).

14           Neutze, R., Wouts, R., van der Spoel, D., Weckert, E. & Hajdu, J. Potential for biomolecular imaging with femtosecond X-ray pulses. Nature 406, 752-757 (2000).

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

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

17           Boutet, S. et al. High-resolution protein structure determination by serial femtosecond crystallography. Science 337, 362-364 (2012).

18           Redecke, L. et al. Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X-ray laser. Science 339, 227-230 (2013).

 

We gratefully acknowledge financial & beamtime support for our research from: