Wikipedia

Janos Hajdu (biophysicist)

Janos Hajdu (born 17 September 1948) is a Swedish/Hungarian scientist, who has made contributions to biochemistry, biophysics, and the science of X-ray free-electron lasers.[13] He is a professor of molecular biophysics at Uppsala University and a leading scientist at the European Extreme Light Infrastructure ERIC in Prague.

Janos Hajdu
Born
Hajdu János Gergely Menyhért

(1948-09-17)17 September 1948
Budapest, Hungary
Education
Alma materEötvös Loránd University (Diploma in Chemistry)
Known for
Scientific career
Fields
Institutions
Doctoral advisor
  • Péter Friedrich [2]
Other academic advisors
Notable students
Websitehttps://lmb.icm.uu.se https://www.eli-beams.eu/?s=elibio

Education

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Hajdu matriculated in 1967 from Eötvös József Gimnasium,[14] a grammar school in Budapest. At the age of 16, he won a science prize, which allowed him to study and perform experiments in the Institute of Medical Chemistry[15] of the Semmelweis University Medical School in Budapest (head: Brunó Ferenc Straub). His first publication was produced in this institute.[16] In 1968, he was admitted to Eötvös Loránd University[17] where he received an M.Sc. in chemistry (1973). He obtained a Ph.D. in biology in 1980, "Symmetry and Structural Changes in Oligomeric Proteins"[18] and a D.Sc. in physics in 1993, "Macromolecular Structure, Function and Dynamics: X-Ray Diffraction Studies in Four Dimensions".[19] He left Hungary in 1981.

Appointments

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  • 2003–present: Professor of Molecular Biophysics, Uppsala University, Sweden.
  • 1995-2003: Professor of Biochemistry, Department of Biochemistry, Uppsala University, Sweden.
  • 2007-2008: Professor of Photon Science, Stanford University, USA.
  • 2016–present: Lead scientist at the European Extreme Light Infrastructure, Dolní Břežany, Czech Republic
  • 2011-2016: Adviser to the Directors of the European XFEL GmbH, Hamburg, Germany.
  • 1988-1996: Head of an MRC Laboratory at the Laboratory of Molecular Biophysics, Oxford, UK.
  • 1988-1996: Lecturer in biochemistry/biophysics, Christ Church, Oxford University, U.K.
  • 1983-1988: MRC/SERC Fellow at the Laboratory of Molecular Biophysics, Oxford Univ., U.K.
  • 1981-1983: EMBO Fellow at the Laboratory of Molecular Biophysics, Oxford Univ., U.K.
  • 1976: Roche fellow, Institute of Medical Chemistry, University of Bern, Switzerland.
  • 1973-2003: Research Fellow, Institute of Enzymology, Hungarian Academy of Sciences, Budapest.

Career and research

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Hajdu's first employment (1973) was with the Institute of Enzymology of the Hungarian Academy of Sciences (head: Brunó Ferenc Straub). In his early work, Hajdu exploited chemistry to determine the symmetry of multi-subunit protein complexes, and characterised structural transitions in these systems.[20][21] Following an invitation by Louise Johnson Hajdu joined Johnson's crystallography team in Oxford in 1981, and spent 16 years in the Laboratory of Molecular Biophysics in Oxford (1981-1996), He was first a postdoctoral research fellow and later the head of an MRC laboratory at the Laboratory of Molecular Biophysics. in 1988, he was elected a lecturer of Christ Church,[22] Oxford, teaching biochemistry and biophysics.

In 1981, the first dedicated Synchrotron Radiation Source came to life in Daresbury,[23] and Hajdu and his colleagues were among the first users of the facility. The new synchrotron gave them the means to pursue a new direction in structural biology which was to not only determine the structure of proteins, but to observe them functioning. The very first time-resolved X-ray diffraction experiments produced 3D movies of catalysis in crystalline enzymes[24][25] and revealed structural transitions in viruses.[26][11] This was a path to understand the workings of molecular machineries, but radiation damage to the sample during exposure was a serious limitation. Hajdu realised there may be a way to outrun radiation damage processes by using extremely short and intense X-ray pulses (speed of light vs. the speed of the shock wave of damage formation).[11] Experimental tests had to wait until the arrival of the first X-ray free-electron lasers,[27][28][29] delivering femtosecond X-ray pulses with a peak brightness exceeding synchrotrons by a factor of ten billion. Funding for building such X-ray free-electron lasers faced hurdles.  

The turning point occurred in 1996, when Hajdu took up a chair at Uppsala University and set up a European research network to explore the physical limits of imaging. The project engaged an interdisciplinary approach, drawing upon structural sciences, plasma physics, optics and mathematics. Hajdu presented their findings to the US Department of Energy in 2000 as part of the scientific justification for building the first hard X-ray free-electron laser, the Linac Coherent Light Source (LCLS), at Stanford.[30][31]

The proof of principle experiment was performed In 2006 with a soft X-ray free-electron laser in Hamburg where Hajdu with Henry N. Chapman and colleagues demonstrated experimentally that outrunning radiation damage is possible with a femtosecond X-ray pulse.[12] The pulse turned the nano-patterned sample into a 60,000 K plasma, but not before a diffraction pattern of the virtually undamaged object could be recorded. The object was reconstructed to the diffraction-limited resolution. When the first hard X-ray free-electron laser (LCLS) was turned on in 2009,[32] they also showed that “diffraction before destruction” or "observation before destruction" extends to the atomic scale [33] launching the methods of serial nano-crystallography,[33] ultrafast diffractive imaging,[34] flash radiography,[35] spectroscopy,[36] and applications in fusion energy research [37][38]

Achievements

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  • X-ray crystallography in four dimensions: First atomic movies on chemical reactions.[39][40]
  • Development of Laue crystallography: First structural results for proteins and viruses.[25][41]
  • Proposal for a link between late steps in protein folding and structural changes in protein function.[42]
  • Discovery of X-ray driven catalysis in redox enzymes.[40]
  • Structures for the family of mononuclear ferrous enzymes.[43][44] 
  • "Diffraction before destruction", the physical limits of imaging.[11][12][45]
  • The scientific case (in imaging) that assured funding for the first hard X-ray free-electron lasers in the US (the LCLS at Stanford) 

[46] and in Europe (the European XFEL, Hamburg).[47][48]

Honours

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  • 2001: Member of the Kungliga Vetenskap-Societeten i Uppsala (The Swedish Royal Society).[51]
  • 2013: Honorary Member, Hungarian Academy of Sciences (2013).[52][53]

Awards

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  • 2022: The Gregori Aminoff Prize (2022)[54][55] for "fundamental contributions to the development of X-ray free-electron laser based structural biology” and "explosive studies of biological macromolecules" together with Henry N. Chapman and John C. H. Spence.
  • 2015: Fabinyi Rudolf Medal "for outstanding contribution to chemistry".[56]
  • 2012: Rudbeck Medal (2012) "for extraordinarily prominent achievements in science, to be conferred primarily for such accomplishments or findings attained at Uppsala University".[57]
  • 2011-2016: ERC Advanced Investigator Award "X-Ray Lasers, Photon Science, and Structural Biology" (XLASERS) ERC 291602.
  • 2011-2016: Knut and Alice Wallenberg Award "Photon Science and X-Ray Lasers (BRIGHT-LIGHT)" KAW 2011.0081.
  • 2005: Centre of Excellence Award, Swedish Research Council.
  • 2001: Excellent Research Environment Award, Swedish Research Council.

Hajdu is Main Editor of the Journal of Applied Crystallography[58] and Editorial Board Member of Nature's Scientific Data.

See also

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References

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  1. ^ https://lcls.slac.stanford.edu/ [bare URL]
  2. ^ Závodszky, Péter (2013). "Péter Friedrich (1936–2013)". FEBS Letters. 587 (9): 1269–1270. Bibcode:2013FEBSL.587.1269Z. doi:10.1016/j.febslet.2013.02.034. PMID 23738340.
  3. ^ https://hu.wikipedia.org/wiki/Cs%C3%A1nyi_Vilmos [bare URL]
  4. ^ https://www.researchgate.net/profile/Pamela-Williams-19 [bare URL]
  5. ^ https://www.icm.uu.se/molecular-biophysics/maia-lab/ [bare URL]
  6. ^ "Filipe R N C Maia".
  7. ^ https://www.researchgate.net/profile/Tove-Sjoegren [bare URL]
  8. ^ https://www.icm.uu.se/molecular-biophysics/ekeberg-lab/ [bare URL]
  9. ^ "Tomas Ekeberg".
  10. ^ https://www.ejg.hu/ [bare URL]
  11. ^ a b c d Neutze, R; Wouts, R; van der Spoel, D; Weckert, E; Hajdu, J (2000). "Potential for femtosecond imaging of biomolecules with X-rays". Nature. 406: 752–757. doi:10.1038/35021099. PMID 10963603.
  12. ^ a b c Chapman, H.N; Barty, A; Bogan, M.J; Boutet, S; Frank, M; Hau-Riege, S.P; Marchesini, S; Woods, B.W; Bajt, S; Benner, W.H; London, R.A; Plönjes, E; Kuhlmann, M; Treusch, R; Düsterer, S; Tschentscher, T; Schneider, J.R; Spiller, E; Möller, T; Bostedt, C; Hoener, M; Shapiro, D.A; Hodgson, K.O; van der Spoel, D; Burmeister, F; Bergh, M; Caleman, C; Huldt, G; Seibert, M.M; Maia, F.R.N.C; Lee, R.W; Szöke, A; Timneanu, N; Hajdu, J (2006). "Femtosecond diffractive imaging with a soft-X-ray free-electron laser". Nature Physics. 2 (12): 839–843. arXiv:physics/0610044. Bibcode:2006NatPh...2..839C. doi:10.1038/nphys461.
  13. ^ "Free-electron laser", Wikipedia, 2024-04-23, retrieved 2024-07-31
  14. ^ "Eötvös József Gimnázium (Budapest)", Wikipédia (in Hungarian), 2024-07-05, retrieved 2024-07-31
  15. ^ "Medical Chemistry". semmelweis.hu. Retrieved 2024-07-31.
  16. ^ Hajdu, J; Csanyi, V (1970). "The influence of concentrated electrolytes on the constitutive penicillinase synthesis of Bacillus cereus". Acta Biochim. Biophys. Acad. Sci. Hung. 5 (1): 41–43. PMID 4992648.
  17. ^ "Eötvös Loránd University". www.elte.hu. Retrieved 2024-07-31.
  18. ^ "PDS bejelentkezés". opac.mtak.hu. Retrieved 2024-07-31.
  19. ^ "PDS bejelentkezés". opac.mtak.hu. Retrieved 2024-07-31.
  20. ^ Hajdu, J; Bartha, F; Friedrich, P (1976-09-15). "Crosslinking with bifunctional reagents as a means for studying the symmetry of oligomeric proteins". Eur J Biochem. 68 (2): 373–383. doi:10.1111/j.1432-1033.1976.tb10824.x. PMID 987906.
  21. ^ Hajdu, J; Dombradi, V; Bot, G; Friedrich, P (1979). "Structural changes in glycogen phosphorylase as revealed by cross-linking with bifunctional diimidates: Phosphorylase b". Biochemistry. 18 (18): 4037–4041. doi:10.1021/bi00585a030. PMID 226120.
  22. ^ "Homepage | Christ Church, University of Oxford". www.chch.ox.ac.uk. Retrieved 2024-07-31.
  23. ^ Synchrotron Radiation Source
  24. ^ Hajdu, J; Acharya, KR; Stuart, DI; McLaughlin, PJ; Barford, D; Oikonomakos, NG; Klein, H; Johnson, LN (1987). "Catalysis in the crystal: synchrotron radiation studies with glycogen phosphorylase b". EMBO J. 6 (2): 539–546. doi:10.1002/j.1460-2075.1987.tb04786.x. PMC 553427. PMID 3107984.
  25. ^ a b Hajdu, J; Machin, PA; Campbell, JW; Greenhough, TJ; Clifton, IJ; Zurek, S; Gover, S; Johnson, LN; Elder, M (1987-09-10). "Millisecond X-ray diffraction and the first electron density map from Laue photographs of a protein crystal". Nature. 329 (6135): 178–181. Bibcode:1987Natur.329..178H. doi:10.1038/329178a0. PMID 3114644.
  26. ^ Campbell, JW; Clifton, IJ; Greenhough, TJ; Hajdu, J; Harrison, SC; Liddington, RC; Shrive, AK (1990). "Calcium binding sites in tomato bushy stunt virus visualized by Laue crystallography". J Mol Biol. 214 (3): 627–632. doi:10.1016/0022-2836(90)90278-T. PMID 2388260.
  27. ^ Free-electron laser
  28. ^ "LCLS | Linac Coherent Light Source | SLAC National Accelerator Laboratory". lcls.slac.stanford.edu. Retrieved 2024-07-31.
  29. ^ European XFEL
  30. ^ Hajdu, J; Hodgson, K; Miao, J; van der Spoel, D; Neutze, R; Robinson, CV; Faigel, G; Jacobsen, C; Kirz, J; Sayre, D; Weckert, E; Materlik, G; Szoke, A (2000). "Structural studies on single particles and biomolecules". SSRL, SLAC, Stanford, USA, SLACR-611. 6: 35–62. doi:10.2172/812649.[1]
  31. ^ Minutes of the October 10–11, 2000 Basic Energy Sciences Advisory Committee (BESAC) meeting.[2]
  32. ^ "LCLS | Linac Coherent Light Source | SLAC National Accelerator Laboratory". lcls.slac.stanford.edu. Retrieved 2024-07-31.
  33. ^ a b Chapman, HN; Fromme, P; Barty, A; White, TA; Kirian, RA; Aquila, A; Hunter, MS; Schulz, J; DePonte, DP; Weierstall, U; Doak, RB; Maia, FR; Martin, AV; Schlichting, I; Lomb, L; Coppola, N; Shoeman, RL; Epp, SW; Hartmann, R; Rolles, D; Rudenko, A; Foucar, L; Kimmel, N; Weidenspointner, G; Holl, P; Liang, M; Barthelmess, M; Caleman, C; Boutet, S; Bogan, MJ; Krzywinski, J (2011). "Femtosecond X-ray protein nanocrystallography". Nature. 470 (7332): 73–7. Bibcode:2011Natur.470...73C. doi:10.1038/nature09750. PMC 3429598. PMID 21293373.
  34. ^ Seibert, MM; Ekeberg, T; Maia, FR; Svenda, M; Andreasson, J; Jönsson, O; Odić, D; Iwan, B; Rocker, A; Westphal, D; Hantke, M; DePonte, DP; Barty, A; Schulz, J; Gumprecht, L; Coppola, N; Aquila, A; Liang, M; White, TA; Martin, A; Caleman, C; Stern, S; Abergel, C; Seltzer, V; Claverie, JM; Potdevin, G; Graafsma, H; Nilsson, B; Chapman, HN; Hajdu, J (2011). "Single mimivirus particles intercepted and imaged with an X-ray laser". Nature. 470 (7332): 78–81. Bibcode:2011Natur.470...78S. doi:10.1038/nature09748. PMC 4038304. PMID 21293374.
  35. ^ Schropp, A; Hoppe, R; Meier, V (2015). "Imaging Shock Waves in Diamond with Both High Temporal and Spatial Resolution at an XFEL". Sci Rep. 5: 11089. Bibcode:2015NatSR...511089S. doi:10.1038/srep11089. PMC 4650669. PMID 26086176.
  36. ^ Roseker, W; Hruszkewycz, SO; Lehmkühler, F (2018). "Towards ultrafast dynamics with split-pulse X-ray photon correlation spectroscopy at free electron laser sources". Nat Commun. 9: 1704. Bibcode:2018NatCo...9.1704R. doi:10.1038/s41467-018-04178-9. PMC 5923200. PMID 29703980.
  37. ^ Radousky, HB; Armstrong, MR; Goldman, N (2021). "Time resolved x-ray diffraction in shock compressed systems". J. Appl. Phys. 129 (4): 040901. Bibcode:2021JAP...129d0901R. doi:10.1063/5.0034929.
  38. ^ Dornheim, T; Böhme, M; Kraus, D; Döppner, T; Preston, TR; Moldabekov, ZA; Vorberger, J (2022). "Accurate temperature diagnostics for matter under extreme conditions". Nat Commun. 13: 7911. arXiv:2206.12805. Bibcode:2022NatCo..13.7911D. doi:10.1038/s41467-022-35578-7. PMID 36564411.
  39. ^ Hajdu, J; Acharya, KR; Stuart, DI; McLaughlin, PJ; Barford, D; Oikonomakos, NG; Klein, H; Johnson, LN (1987). "Catalysis in the crystal: synchrotron radiation studies with glycogen phosphorylase b". EMBO J. 6 (2): 539–546. doi:10.1002/j.1460-2075.1987.tb04786.x. PMC 553427. PMID 3107984.
  40. ^ a b Berglund, GI; Carlsson, GH; Smith, AT; Szöke, H; Henriksen, A; Hajdu, J (2002). "The catalytic pathway of horseradish peroxidase at high resolution". Nature. 417 (6887): 463–468. Bibcode:2002Natur.417..463B. doi:10.1038/417463a. PMID 12024218.
  41. ^ Campbell, JW; Clifton, IJ; Greenhough, TJ; Hajdu, J; Harrison, SC; Liddington, RC; Shrive, AK (1990). "Calcium binding sites in tomato bushy stunt virus visualized by Laue crystallography". J. Mol. Biol. 214 (3): 627–632. doi:10.1016/0022-2836(90)90278-T. PMID 2388260.
  42. ^ Williams, PA; Fülöp, V; Garman, EF; Saunders, NF; Ferguson, SJ; Hajdu, J (1997-09-25). "Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme". Nature. 389 (6649): 406–412. Bibcode:1997Natur.389..406W. doi:10.1038/38775. PMID 9311786.
  43. ^ Roach, PL; Clifton, IJ; Fülöp, V; Harlos, K; Barton, GJ; Hajdu, J; Andersson, I; Schofield, CJ; Baldwin, JE (1995-06-22). "Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes". Nature. 375 (6533): 700–704. Bibcode:1995Natur.375..700R. doi:10.1038/375700a0. PMID 7791906.
  44. ^ Valegård, K; van Scheltinga, AC; Lloyd, MD; Hara, T; Ramaswamy, S; Perrakis, A; Thompson, A; Lee, HJ; Baldwin, JE; Schofield, CJ; Hajdu, J; Andersson, I (1998-08-20). "Structure of a cephalosporin synthase". Nature. 394 (6695): 805–809. Bibcode:1998Natur.394..805V. doi:10.1038/29575. PMID 9723623.
  45. ^ Chapman, HN; Hau-Riege, SP; Bogan, MJ; Bajt, S; Barty, A; Boutet, S; Marchesini, S; Frank, M; Woods, BW; Benner, WH; London, RA; Rohner, U; Szöke, A; Spiller, E; Möller, T; Bostedt, C; Shapiro, DA; Kuhlmann, M; Treusch, R; Plönjes, E; Burmeister, F; Bergh, M; Caleman, C; Huldt, G; Seibert, MM; Hajdu, J (2007-08-09). "Femtosecond time-delay X-ray holography". Nature. 448 (7154): 676–679. Bibcode:2007Natur.448..676C. doi:10.1038/nature06049. PMID 17687320.
  46. ^ Hajdu, J., Hodgson, K., Miao, J., van der Spoel, D., Neutze, R., Robinson, C.V., Faigel, G., Jacobsen, C., Kirz, J., Sayre, D., Weckert, E., Materlik, G., Szoke, A. Structural studies on single particles and biomolecules. In LCLS: The First Experiments. pp. 35-62. Published in 2000 by SSRL, SLAC, Stanford, USA, SLAC-R-611 (2000). [3][4]
  47. ^ Hajdu, J; Chapman, HN (2006). Ultrafast coherent diffraction imaging of single particles, clusters and biomolecules. Technical Design Report (Report). DESY 2006-097. Verlag: Deutsches Elektronen-Synchrotron. pp. 352–386. doi:10.2172/900146. ISBN 3935702175.
  48. ^ Altarelli, M; Brinkmann, R; Chergui, M; Decking, W; Dobson, B; Düsterer, S; Grübel, G; Graeff, W; Graafsma, H; Hajdu, J; Marangos, J; Pflüger, J; Redlin, H; Riley, D; Robinson, I; Rossbach, J; Schwarz, A; Tiedtke, K; Tschentscher, T; Vartaniants, I; Wabnitz, H; Weise, H; Wichmann, R; Witte, K; Wolf, A; Wulff, M; Yurkov, M (2006). The European x-ray free-electron laser (Report). DESY 2006-097. doi:10.3204/DESY_06-097. ISBN 3935702175.
  49. ^ https://eli-laser.eu/media/1019/eli-whitebook.pdf [bare URL PDF]
  50. ^ Tajima, T., Barish, B., Barty, C., Bulanov, S., Chen, P., Feldhaus, J., Hajdu, J., Keitel, C., Kieffer, J., Ko, D., Leemans, W., Normand, D., Palumbo, L., Rzazewski, K., Sergeev, A., Sheng, Z., Takasaki, F., and Teshima, M., Science of Extreme Light Infrastructure, in AIP Proceedings 1228 “Light at Extreme Intensities Opportunities and Technological Issues of the Extreme Light Infrastructure”, ed. D. Dumitras, AIP, NY (2010). [5]
  51. ^ "Kungl. Vetenskaps-Societeten".
  52. ^ https://mta.hu/ [bare URL]
  53. ^ "Köztestületi tagok".
  54. ^ "Aminoff Prize rewards explosive studies of biological macromolecules". 14 September 2020.
  55. ^ "Royal honour for Professor Janos Hajdu of Uppsala University | Laboratory of Molecular Biophysics". 17 June 2022.
  56. ^ "Fabinyi Rudolf Emlékérem".
  57. ^ "The Rudbeck Medal - Uppsala University". 21 August 2024.
  58. ^ "(IUCr) Journal of Applied Crystallography".
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