Indications of radiation damage in ferredoxin microcrystals using high-intensity X-FEL beams

Karol Nass, Lutz Foucar, Thomas R.M. Barends, Elisabeth Hartmann, Sabine Botha, Robert L. Shoeman, R. Bruce Doak, Roberto Alonso-Mori, Andrew Aquila, Saša Bajt, Anton Barty, Richard Bean, Kenneth R. Beyerlein, Maike Bublitz, Nikolaj Drachmann, Jonas Gregersen, H. Olof Jönsson, Wolfgang Kabsch, Stephan Kassemeyer, Jason E. Koglin & 14 others Michael Krumrey, Daniel Mattle, Marc Messerschmidt, Poul Nissen, Linda Reinhard, Oleg Sitsel, Dimosthenis Sokaras, Garth J. Williams, Stefan Hau-Riege, Nicusor Timneanu, Carl Caleman, Henry N. Chapman, Sébastien Boutet, Ilme Schlichting

Research output: Contribution to journalConference article

69 Citations (Scopus)

Abstract

Proteins that contain metal cofactors are expected to be highly radiation sensitive since the degree of X-ray absorption correlates with the presence of high-atomic-number elements and X-ray energy. To explore the effects of local damage in serial femtosecond crystallography (SFX), Clostridium ferredoxin was used as a model system. The protein contains two [4Fe-4S] clusters that serve as sensitive probes for radiation-induced electronic and structural changes. High-dose room-temperature SFX datasets were collected at the Linac Coherent Light Source of ferredoxin microcrystals. Difference electron density maps calculated from high-dose SFX and synchrotron data show peaks at the iron positions of the clusters, indicative of decrease of atomic scattering factors due to ionization. The electron density of the two [4Fe-4S] clusters differs in the FEL data, but not in the synchrotron data. Since the clusters differ in their detailed architecture, this observation is suggestive of an influence of the molecular bonding and geometry on the atomic displacement dynamics following initial photoionization. The experiments are complemented by plasma code calculations.

Original languageEnglish (US)
Pages (from-to)225-238
Number of pages14
JournalJournal of Synchrotron Radiation
Volume22
Issue number2
DOIs
StatePublished - Jan 1 2015
Externally publishedYes
Event8th International Workshop on X-ray Radiation Damage to Biological Crystalline Samples - Hamburg, Germany
Duration: Apr 10 2014Apr 12 2014

Fingerprint

Microcrystals
Free electron lasers
microcrystals
Radiation damage
Synchrotrons
radiation damage
Carrier concentration
indication
Proteins
Radiation
Clostridium
Photoionization
Crystallography
Lattice vibrations
X ray absorption
Dosimetry
Ionization
Light sources
synchrotrons
Iron

Keywords

  • free-electron laser
  • metalloprotein Includes papers presented at the 8th International Workshop on X-ray Radiation Damage to Biological Crystalline Samples
  • protein crystallography
  • radiation damage
  • serial femtosecond crystallography
  • SFX

ASJC Scopus subject areas

  • Radiation
  • Nuclear and High Energy Physics
  • Instrumentation

Cite this

Nass, K., Foucar, L., Barends, T. R. M., Hartmann, E., Botha, S., Shoeman, R. L., ... Schlichting, I. (2015). Indications of radiation damage in ferredoxin microcrystals using high-intensity X-FEL beams. Journal of Synchrotron Radiation, 22(2), 225-238. https://doi.org/10.1107/S1600577515002349

Indications of radiation damage in ferredoxin microcrystals using high-intensity X-FEL beams. / Nass, Karol; Foucar, Lutz; Barends, Thomas R.M.; Hartmann, Elisabeth; Botha, Sabine; Shoeman, Robert L.; Doak, R. Bruce; Alonso-Mori, Roberto; Aquila, Andrew; Bajt, Saša; Barty, Anton; Bean, Richard; Beyerlein, Kenneth R.; Bublitz, Maike; Drachmann, Nikolaj; Gregersen, Jonas; Jönsson, H. Olof; Kabsch, Wolfgang; Kassemeyer, Stephan; Koglin, Jason E.; Krumrey, Michael; Mattle, Daniel; Messerschmidt, Marc; Nissen, Poul; Reinhard, Linda; Sitsel, Oleg; Sokaras, Dimosthenis; Williams, Garth J.; Hau-Riege, Stefan; Timneanu, Nicusor; Caleman, Carl; Chapman, Henry N.; Boutet, Sébastien; Schlichting, Ilme.

In: Journal of Synchrotron Radiation, Vol. 22, No. 2, 01.01.2015, p. 225-238.

Research output: Contribution to journalConference article

Nass, K, Foucar, L, Barends, TRM, Hartmann, E, Botha, S, Shoeman, RL, Doak, RB, Alonso-Mori, R, Aquila, A, Bajt, S, Barty, A, Bean, R, Beyerlein, KR, Bublitz, M, Drachmann, N, Gregersen, J, Jönsson, HO, Kabsch, W, Kassemeyer, S, Koglin, JE, Krumrey, M, Mattle, D, Messerschmidt, M, Nissen, P, Reinhard, L, Sitsel, O, Sokaras, D, Williams, GJ, Hau-Riege, S, Timneanu, N, Caleman, C, Chapman, HN, Boutet, S & Schlichting, I 2015, 'Indications of radiation damage in ferredoxin microcrystals using high-intensity X-FEL beams', Journal of Synchrotron Radiation, vol. 22, no. 2, pp. 225-238. https://doi.org/10.1107/S1600577515002349
Nass, Karol ; Foucar, Lutz ; Barends, Thomas R.M. ; Hartmann, Elisabeth ; Botha, Sabine ; Shoeman, Robert L. ; Doak, R. Bruce ; Alonso-Mori, Roberto ; Aquila, Andrew ; Bajt, Saša ; Barty, Anton ; Bean, Richard ; Beyerlein, Kenneth R. ; Bublitz, Maike ; Drachmann, Nikolaj ; Gregersen, Jonas ; Jönsson, H. Olof ; Kabsch, Wolfgang ; Kassemeyer, Stephan ; Koglin, Jason E. ; Krumrey, Michael ; Mattle, Daniel ; Messerschmidt, Marc ; Nissen, Poul ; Reinhard, Linda ; Sitsel, Oleg ; Sokaras, Dimosthenis ; Williams, Garth J. ; Hau-Riege, Stefan ; Timneanu, Nicusor ; Caleman, Carl ; Chapman, Henry N. ; Boutet, Sébastien ; Schlichting, Ilme. / Indications of radiation damage in ferredoxin microcrystals using high-intensity X-FEL beams. In: Journal of Synchrotron Radiation. 2015 ; Vol. 22, No. 2. pp. 225-238.
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abstract = "Proteins that contain metal cofactors are expected to be highly radiation sensitive since the degree of X-ray absorption correlates with the presence of high-atomic-number elements and X-ray energy. To explore the effects of local damage in serial femtosecond crystallography (SFX), Clostridium ferredoxin was used as a model system. The protein contains two [4Fe-4S] clusters that serve as sensitive probes for radiation-induced electronic and structural changes. High-dose room-temperature SFX datasets were collected at the Linac Coherent Light Source of ferredoxin microcrystals. Difference electron density maps calculated from high-dose SFX and synchrotron data show peaks at the iron positions of the clusters, indicative of decrease of atomic scattering factors due to ionization. The electron density of the two [4Fe-4S] clusters differs in the FEL data, but not in the synchrotron data. Since the clusters differ in their detailed architecture, this observation is suggestive of an influence of the molecular bonding and geometry on the atomic displacement dynamics following initial photoionization. The experiments are complemented by plasma code calculations.",
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T1 - Indications of radiation damage in ferredoxin microcrystals using high-intensity X-FEL beams

AU - Nass, Karol

AU - Foucar, Lutz

AU - Barends, Thomas R.M.

AU - Hartmann, Elisabeth

AU - Botha, Sabine

AU - Shoeman, Robert L.

AU - Doak, R. Bruce

AU - Alonso-Mori, Roberto

AU - Aquila, Andrew

AU - Bajt, Saša

AU - Barty, Anton

AU - Bean, Richard

AU - Beyerlein, Kenneth R.

AU - Bublitz, Maike

AU - Drachmann, Nikolaj

AU - Gregersen, Jonas

AU - Jönsson, H. Olof

AU - Kabsch, Wolfgang

AU - Kassemeyer, Stephan

AU - Koglin, Jason E.

AU - Krumrey, Michael

AU - Mattle, Daniel

AU - Messerschmidt, Marc

AU - Nissen, Poul

AU - Reinhard, Linda

AU - Sitsel, Oleg

AU - Sokaras, Dimosthenis

AU - Williams, Garth J.

AU - Hau-Riege, Stefan

AU - Timneanu, Nicusor

AU - Caleman, Carl

AU - Chapman, Henry N.

AU - Boutet, Sébastien

AU - Schlichting, Ilme

PY - 2015/1/1

Y1 - 2015/1/1

N2 - Proteins that contain metal cofactors are expected to be highly radiation sensitive since the degree of X-ray absorption correlates with the presence of high-atomic-number elements and X-ray energy. To explore the effects of local damage in serial femtosecond crystallography (SFX), Clostridium ferredoxin was used as a model system. The protein contains two [4Fe-4S] clusters that serve as sensitive probes for radiation-induced electronic and structural changes. High-dose room-temperature SFX datasets were collected at the Linac Coherent Light Source of ferredoxin microcrystals. Difference electron density maps calculated from high-dose SFX and synchrotron data show peaks at the iron positions of the clusters, indicative of decrease of atomic scattering factors due to ionization. The electron density of the two [4Fe-4S] clusters differs in the FEL data, but not in the synchrotron data. Since the clusters differ in their detailed architecture, this observation is suggestive of an influence of the molecular bonding and geometry on the atomic displacement dynamics following initial photoionization. The experiments are complemented by plasma code calculations.

AB - Proteins that contain metal cofactors are expected to be highly radiation sensitive since the degree of X-ray absorption correlates with the presence of high-atomic-number elements and X-ray energy. To explore the effects of local damage in serial femtosecond crystallography (SFX), Clostridium ferredoxin was used as a model system. The protein contains two [4Fe-4S] clusters that serve as sensitive probes for radiation-induced electronic and structural changes. High-dose room-temperature SFX datasets were collected at the Linac Coherent Light Source of ferredoxin microcrystals. Difference electron density maps calculated from high-dose SFX and synchrotron data show peaks at the iron positions of the clusters, indicative of decrease of atomic scattering factors due to ionization. The electron density of the two [4Fe-4S] clusters differs in the FEL data, but not in the synchrotron data. Since the clusters differ in their detailed architecture, this observation is suggestive of an influence of the molecular bonding and geometry on the atomic displacement dynamics following initial photoionization. The experiments are complemented by plasma code calculations.

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KW - metalloprotein Includes papers presented at the 8th International Workshop on X-ray Radiation Damage to Biological Crystalline Samples

KW - protein crystallography

KW - radiation damage

KW - serial femtosecond crystallography

KW - SFX

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