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Abstract: T21.00010 : Protein molecular deformation and protein crystal damage induced by shock waves traveling in liquid microjets. 2:37 PM–2:50 PM

MPS-Authors
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Grünbein,  Marie L
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Foucar,  Lutz
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Gorel,  Alexander
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Hilpert,  Mario
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Kloos,  Marco
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Nass,  Karol
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Nass Kovács,  Gabriela
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Roome,  Christopher M
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Shoeman,  Robert L
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Stricker,  Miriam
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Doak,  R. Bruce
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Barends,  Thomas R. M.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Schlichting,  Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

https://meetings.aps.org/Meeting/DFD21/Session/T21.10
(Abstract)

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Citation

Stan, C. A., Grünbein, M. L., Foucar, L., Gorel, A., Hilpert, M., Kloos, M., et al. (2021). Abstract: T21.00010: Protein molecular deformation and protein crystal damage induced by shock waves traveling in liquid microjets. 2:37 PM–2:50 PM. Bulletin of the American Physical Society.


Cite as: https://hdl.handle.net/21.11116/0000-0009-4579-2
Abstract
Femtosecond crystallography studies done at X-ray laser facilities are an emerging method that provides new insights into the biological function of complex proteins. Second-generation X-ray lasers enable acquisition rates exceeding a million diffraction images per second, and to supply fresh protein crystals at these rates, they must be carried by high-velocity liquid microjets. These microjets also guide the shock waves generated by previous X-ray pulses. The effect of shocks generated by previous X-ray pulses on lysozyme and carboxyhemoglobin crystals was investigated experimentally. The molecular structure of the lysozyme did not change after shocks with amplitudes up to 140 MPa, but the quality of diffraction data decreased for shocks above 30−45 MPa, indicating crystal damage. In contrast, the molecular structure of carboxyhemoglobin changed after shocks ranging from 35 to 70 MPa. These results suggest the shocks induced brittle failure in lysozyme but plastic deformation in carboxyhemoglobin, and were used to estimate under what conditions X-ray laser crystallography data is likely to be affected by such shocks.