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

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Title: Electronic damage in S atoms in a native protein crystal induced by an intense X-ray free-electron laser pulse.
Authors: Galli, L.1,2, Son1,3, Klinge, M.4, Bajt, S.5, Barty, A.1, Bean, R.1, Betzel, C.6, Beyerlein, K. R.1, Caleman, C.1,7, Doak, R. B.8, Duszenko, M.9, Fleckenstein, H.1, Gati, C.1, Hunt, B.10, Kirian, R. A.1, Liang, M.1, Nanao, M. H.11, Nass, K.8, Oberthür, D.1, Redecke, L.4
Source: Structural Dynamics. 2015, Vol. 2 Issue 4, p1-8. 8p.
Subjects: Radiation damage, Crystalloids (Botany), X-rays, Free electron lasers, Radiation doses
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. [ABSTRACT FROM AUTHOR]
Copyright of Structural Dynamics is the property of American Institute of Physics and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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DbLabel: Engineering Source
An: 109330249
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PubType: Academic Journal
PubTypeId: academicJournal
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  Data: Electronic damage in S atoms in a native protein crystal induced by an intense X-ray free-electron laser pulse.
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  Data: <searchLink fieldCode="JN" term="%22Structural+Dynamics%22">Structural Dynamics</searchLink>. 2015, Vol. 2 Issue 4, p1-8. 8p.
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  Data: <searchLink fieldCode="DE" term="%22Radiation+damage%22">Radiation damage</searchLink><br /><searchLink fieldCode="DE" term="%22Crystalloids+%28Botany%29%22">Crystalloids (Botany)</searchLink><br /><searchLink fieldCode="DE" term="%22X-rays%22">X-rays</searchLink><br /><searchLink fieldCode="DE" term="%22Free+electron+lasers%22">Free electron lasers</searchLink><br /><searchLink fieldCode="DE" term="%22Radiation+doses%22">Radiation doses</searchLink>
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  Data: 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. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Structural Dynamics is the property of American Institute of Physics and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1063/1.4919398
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