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Crystal structures of the Bacillus subtilis prophage lytic cassette proteins XepA and YomS

Freitag-Pohl, Stefanie; Jasilionis, Andrius; Håkansson, Maria; Svensson, L. Anders; Kovačič, Rebeka; Welin, Martin; Watzlawick, Hildegard; Wang, Lei; Altenbuchner, Josef; Płotka, Magdalena; Kaczorowska, Anna Karina; Kaczorowski, Tadeusz; Nordberg Karlsson, Eva; Al-Karadaghi, Salam; Walse, Björn; Aevarsson, Arnthór; Pohl, Ehmke

Crystal structures of the Bacillus subtilis prophage lytic cassette proteins XepA and YomS Thumbnail


Authors

Andrius Jasilionis

Maria Håkansson

L. Anders Svensson

Rebeka Kovačič

Martin Welin

Hildegard Watzlawick

Lei Wang

Josef Altenbuchner

Magdalena Płotka

Anna Karina Kaczorowska

Tadeusz Kaczorowski

Eva Nordberg Karlsson

Salam Al-Karadaghi

Björn Walse

Arnthór Aevarsson



Abstract

For the extraction of the best possible X-ray diffraction data from macromolecular crystals, accurate positioning of the crystals with respect to the X-ray beam is crucial. In addition, information about the shape and internal defects of crystals allows the optimization of data-collection strategies. Here, it is demonstrated that the X-ray beam available on the macromolecular crystallo­graphy beamline P14 at the high-brilliance synchrotron-radiation source PETRA III at DESY, Hamburg, Germany can be used for high-energy phase-contrast microtomography of protein crystals mounted in an optically opaque lipidic cubic phase matrix. Three-dimensional tomograms have been obtained at X-ray doses that are substantially smaller and on time scales that are substantially shorter than those used for diffraction-scanning approaches that display protein crystals at micrometre resolution. Adding a compound refractive lens as an objective to the imaging setup, two-dimensional imaging at sub-micrometre resolution has been achieved. All experiments were performed on a standard macromolecular crystallography beamline and are compatible with standard diffraction data-collection workflows and apparatus. Phase-contrast X-ray imaging of macromolecular crystals could find wide application at existing and upcoming low-emittance synchrotron-radiation sources.

Citation

Freitag-Pohl, S., Jasilionis, A., Håkansson, M., Svensson, L. A., Kovačič, R., Welin, M., …Pohl, E. (2019). Crystal structures of the Bacillus subtilis prophage lytic cassette proteins XepA and YomS. Acta Crystallographica Section D: Structural Biology, 75(11), 1028-1039. https://doi.org/10.1107/s2059798319013330

Journal Article Type Article
Acceptance Date Sep 28, 2019
Publication Date Nov 1, 2019
Deposit Date Nov 11, 2019
Publicly Available Date Nov 13, 2019
Journal Acta crystallographica. Section D, Structural biology.
Print ISSN 2059-7983
Publisher International Union of Crystallography
Peer Reviewed Peer Reviewed
Volume 75
Issue 11
Pages 1028-1039
DOI https://doi.org/10.1107/s2059798319013330

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Publisher Licence URL
http://creativecommons.org/licenses/by/4.0/

Copyright Statement
Supplementary information This is an Open Access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution and reproduction in any medium, provided the original authors and source are cited.





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