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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

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.

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 Creators:
Stan, Claudiu A, Author
Grünbein, Marie L1, Author              
Foucar, Lutz1, Author              
Gorel, Alexander1, Author              
Hilpert, Mario1, Author              
Kloos, Marco1, Author              
Nass, Karol1, Author              
Nass Kovács, Gabriela1, Author              
Roome, Christopher M1, Author              
Shoeman, Robert L1, Author              
Stricker, Miriam1, Author              
Carbajo, Sergio, Author
Colocho, William, Author
Gilevich, Sasha, Author
Hunter, Mark, Author
Lewandowski, Jim, Author
Lutman, Alberto, Author
Koglin, Jason E, Author
Lane, Thomas J, Author
van Driel, Tim, Author
Sheppard, John, AuthorVetter, Sharon L, AuthorTurner, James, AuthorDoak, R. Bruce1, Author              Barends, Thomas R. M.1, Author              Boutet, Sebastien, AuthorAquila, Andrew L, AuthorDecker, Franz J, AuthorSchlichting, Ilme1, Author               more..
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 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.

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 Dates: 2021
 Publication Status: Published online
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Title: 74th Annual Meeting of the APS Division of Fluid Dynamics
Place of Event: Phoenix Convention Center, Phoenix, Arizona
Start-/End Date: 2021-11-21 - 2021-11-23

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Title: Bulletin of the American Physical Society
Source Genre: Journal
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Publ. Info: New York : Published by the American Institute of Physics for the American Physical Society [etc.]
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: - Identifier: ISSN: 0003-0503
CoNE: https://pure.mpg.de/cone/journals/resource/110978979593673