Current hard X-ray free-electron laser (XFEL) sources can deliver doses to biological macromolecules well exceeding 1 GGy, in timescales of a few tens of femtoseconds. During the pulse, photoionization can reach the point of saturation in which certain atomic species in the sample lose most of their electrons. This electronic radiation damage causes the atomic scattering factors to change, affecting, in particular, the heavy atoms, due to their higher photoabsorption cross sections. Here, it is shown that experimental serial femtosecond crystallography data collected with an extremely bright XFEL source exhibit a reduction of the effective scattering power of the sulfur atoms in a native protein. Quantitative methods are developed to retrieve information on the effective ionization of the damaged atomic species from experimental data, and the implications of utilizing new phasing methods which can take advantage of this localized radiation damage are discussed.

Galli, L., Son, S.-., Klinge, M., Bajt, S., Barty, A., Bean, R., et al. (2015). Electronic damage in S atoms in a native protein crystal induced by an intense X-ray free-electron laser pulse. STRUCTURAL DYNAMICS, 2(4) [10.1063/1.4919398].

Electronic damage in S atoms in a native protein crystal induced by an intense X-ray free-electron laser pulse

Stellato F.
Investigation
;
2015-01-01

Abstract

Current hard X-ray free-electron laser (XFEL) sources can deliver doses to biological macromolecules well exceeding 1 GGy, in timescales of a few tens of femtoseconds. During the pulse, photoionization can reach the point of saturation in which certain atomic species in the sample lose most of their electrons. This electronic radiation damage causes the atomic scattering factors to change, affecting, in particular, the heavy atoms, due to their higher photoabsorption cross sections. Here, it is shown that experimental serial femtosecond crystallography data collected with an extremely bright XFEL source exhibit a reduction of the effective scattering power of the sulfur atoms in a native protein. Quantitative methods are developed to retrieve information on the effective ionization of the damaged atomic species from experimental data, and the implications of utilizing new phasing methods which can take advantage of this localized radiation damage are discussed.
2015
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore FIS/07 - FISICA APPLICATA (A BENI CULTURALI, AMBIENTALI, BIOLOGIA E MEDICINA)
English
Galli, L., Son, S.-., Klinge, M., Bajt, S., Barty, A., Bean, R., et al. (2015). Electronic damage in S atoms in a native protein crystal induced by an intense X-ray free-electron laser pulse. STRUCTURAL DYNAMICS, 2(4) [10.1063/1.4919398].
Galli, L; Son, S-; Klinge, M; Bajt, S; Barty, A; Bean, R; Betzel, C; Beyerlein, Kr; Caleman, C; Doak, Rb; Duszenko, M; Fleckenstein, H; Gati, C; Hunt, B; Kirian, Ra; Liang, M; Nanao, Mh; Nass, K; Oberthur, D; Redecke, L; Shoeman, R; Stellato, F; Yoon, Ch; White, Ta; Yefanov, O; Spence, J; Chapman, Hn
Articolo su rivista
File in questo prodotto:
File Dimensione Formato  
Galli-StructDyn2015.pdf

accesso aperto

Tipologia: Versione Editoriale (PDF)
Licenza: Creative commons
Dimensione 1.17 MB
Formato Adobe PDF
1.17 MB Adobe PDF Visualizza/Apri

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/266654
Citazioni
  • ???jsp.display-item.citation.pmc??? 3
  • Scopus 19
  • ???jsp.display-item.citation.isi??? 16
social impact